Target Information
| Target General Information | Top | |||||
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| Target ID |
T08123
(Former ID: TTDI03347)
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| Target Name |
Leucine-rich repeat kinase 2 (LRRK2)
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| Synonyms |
PARK8; Leucine-rich repeat serine/threonine-protein kinase 2; Dardarin
Click to Show/Hide
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| Gene Name |
LRRK2
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| Target Type |
Clinical trial target
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[1] | ||||
| Disease | [+] 1 Target-related Diseases | + | ||||
| 1 | Parkinsonism [ICD-11: 8A00] | |||||
| Function |
Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease. Plays an important role in recuiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization.
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| BioChemical Class |
Kinase
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| UniProt ID | ||||||
| EC Number |
EC 2.7.11.1
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| Sequence |
MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNI
HVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILK MLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLG CKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVE VLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQ QYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWH RKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASAN ALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIM AAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKN DIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQ EIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSA SFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQN NSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIG KGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLA RMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEG SFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLR SSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQ NALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTV KCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNH ISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRS LDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEI PPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIR FLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQI RDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKA RASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKL RKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVREN QLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPK HPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVI ELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYL NWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDI CGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLI LADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQE LVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVAD GLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRA PEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYG CAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHH NSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQ SGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTV KLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRT SQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKE NKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMT AQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEK MRRTSVE Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| HIT2.0 ID | T11TKN | |||||
| Drugs and Modes of Action | Top | |||||
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| Clinical Trial Drug(s) | [+] 3 Clinical Trial Drugs | + | ||||
| 1 | BIIB094 | Drug Info | Phase 1 | Parkinson disease | [2] | |
| 2 | DNL151 | Drug Info | Phase 1 | Parkinson disease | [1] | |
| 3 | DNL201 | Drug Info | Phase 1 | Parkinson disease | [1] | |
| Mode of Action | [+] 1 Modes of Action | + | ||||
| Inhibitor | [+] 41 Inhibitor drugs | + | ||||
| 1 | BIIB094 | Drug Info | [3] | |||
| 2 | DNL151 | Drug Info | [1] | |||
| 3 | DNL201 | Drug Info | [1] | |||
| 4 | Aminopyridine derivative 2 | Drug Info | [4] | |||
| 5 | Aminopyridine derivative 3 | Drug Info | [4] | |||
| 6 | Azaindazole derivative 1 | Drug Info | [4] | |||
| 7 | Azaindazole derivative 2 | Drug Info | [4] | |||
| 8 | Azaindazole derivative 3 | Drug Info | [4] | |||
| 9 | Azaindazole derivative 4 | Drug Info | [4] | |||
| 10 | Bidentate ligands of Markush derivative 1 | Drug Info | [4] | |||
| 11 | Bidentate ligands of Markush derivative 2 | Drug Info | [4] | |||
| 12 | Fused thiophene derivative 1 | Drug Info | [4] | |||
| 13 | Hydrazide derivative 3 | Drug Info | [4] | |||
| 14 | Hydrazide derivative 4 | Drug Info | [4] | |||
| 15 | Hydrazide derivative 5 | Drug Info | [4] | |||
| 16 | Oxindole derivative 2 | Drug Info | [4] | |||
| 17 | Oxindole derivative 3 | Drug Info | [4] | |||
| 18 | Oxindole derivative 4 | Drug Info | [4] | |||
| 19 | PMID28117607-Compound-20 | Drug Info | [4] | |||
| 20 | PMID28117607-Compound-21 | Drug Info | [4] | |||
| 21 | PMID28117607-Compound-4 | Drug Info | [4] | |||
| 22 | PMID28117607-Compound-5 | Drug Info | [4] | |||
| 23 | PMID28117607-Compound-6 | Drug Info | [4] | |||
| 24 | PMID28117607-Compound-7 | Drug Info | [4] | |||
| 25 | Pyridopyrimidinone derivative 1 | Drug Info | [4] | |||
| 26 | Pyridopyrimidinone derivative 2 | Drug Info | [4] | |||
| 27 | Pyridopyrimidinone derivative 3 | Drug Info | [4] | |||
| 28 | Pyrrolo-pyridazine derivative 1 | Drug Info | [4] | |||
| 29 | Pyrrolo-pyridine derivative 1 | Drug Info | [4] | |||
| 30 | Pyrrolo-pyridine derivative 2 | Drug Info | [4] | |||
| 31 | Pyrrolo-pyrimidine derivative 1 | Drug Info | [4] | |||
| 32 | Pyrrolo-pyrimidine derivative 10 | Drug Info | [4] | |||
| 33 | Pyrrolo-pyrimidine derivative 11 | Drug Info | [4] | |||
| 34 | Pyrrolo-pyrimidine derivative 8 | Drug Info | [4] | |||
| 35 | Pyrrolo-pyrimidine derivative 9 | Drug Info | [4] | |||
| 36 | GNE-7915 | Drug Info | [5] | |||
| 37 | GNE-9605 | Drug Info | [5] | |||
| 38 | HMS3229G13 | Drug Info | [6] | |||
| 39 | PF-06447475 | Drug Info | [7] | |||
| 40 | PF-06454589 | Drug Info | [7] | |||
| 41 | URMC-099 | Drug Info | [8] | |||
| Cell-based Target Expression Variations | Top | |||||
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| Cell-based Target Expression Variations | ||||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: Adenosine triphosphate | Ligand Info | |||||
| Structure Description | Structure of LRRK2 after symmetry expansion | PDB:7LI4 | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | Yes | [9] |
| PDB Sequence |
GIQKCGLKVI
567 SSIVHFPDAL577 GAMDSVLHTL593 QMYPDDQEIQ603 CLGLSLIGYG624 HLLAKILVSS 634 LYRFKDVAEI644 QTKGFQTILA654 ILKLSASFSK664 LLVHHSFDLV674 IFHQMSSNIM 684 EQKDQQFLNL694 CCKCFAKVAM704 DDYLKNVMLE714 RACDQNNSIM724 VECLLLLGAD 734 ANQAKEGSSL744 ICQVCEKESS754 PKLVELLLNS764 GSREQDVRKA774 LTISIGKGDS 784 QIISLLLRRL794 ALDVANNSIC804 LGGFCIGKVE814 PSWLGPLFPD824 KTSNLRKQTN 834 IASTLARMVI844 RYQMKSAVEE854 REYITSLDLS990 ANELRDIDAL1000 SQKCCISVHL 1010 EHLEKLELHQ1020 NALTSFPQQL1030 CETLKSLTHL1040 DLHSNKFTSF1050 PSYLLKMSCI 1060 ANLDVSRNDI1070 GPSVVLDPTV1080 KCPTLKQFNL1090 SYNQLSFVPE1100 NLTDVVEKLE 1110 QLILEGNKIS1120 GICSPLRLKE1130 LKILNLSKNH1140 ISSLSENFLE1150 ACPKVESFSA 1160 RMNFLAAMPF1170 LPPSMTILKL1180 SQNKFSCIPE1190 AILNLPHLRS1200 LDMSSNDIQY 1210 LPGPAHWKSL1220 NLRELLFSHN1230 QISILDLSEK1240 AYLWSRVEKL1250 HLSHNKLKEI 1260 PPEIGCLENL1270 TSLDVSYNLE1280 LRSFPNEMGK1290 LSKIWDLPLD1300 ELHLNFDFKH 1310 IGCKAKDIIR1320 FLQQRLKKAV1330 PYNRMKLMIV1340 GNTGSGKTTL1350 LQQLMKTKKS 1360 DLGMQSATVG1370 IDVKDWPIQI1380 RDKRKRDLVL1390 NVWDFAGREE1400 FYSTHPHFMT 1410 QRALYLAVYD1420 LSKGQAEVDA1430 MKPWLFNIKA1440 RASSSPVILV1450 GTHLDVSKAC 1465 MSKITKELLN1475 KRGFPAIRDY1485 HFVNATEESD1495 ALAKLRKTII1505 NESLNFKIRD 1515 QLVVGQLIPD1525 CYVELEKIIL1535 SERKNVPIEF1545 PVIDRKRLLQ1555 LVRENQLQLD 1565 ENELPHAVHF1575 LNESGVLLHF1585 QDPALQLSDL1595 YFVEPKWLCK1605 IMAQILTVKV 1615 EGCPKHPKGI1625 ISRRDPKNYM1646 TQYFKLLEKF1656 QIALVPSSLS1674 DHRPVIELPH 1684 CENSEIIIRL1694 YEMPYFPMGF1704 WSRLINRLLE1714 ISPYMLALRP1729 NRMYWRQGIY 1739 LNWSPEAYCL1749 VGSEVLDNHP1759 ESFLKITVPS1769 CRKGCILLGQ1779 VVDHIDSLME 1789 EWFPGLLEID1799 ICGEGETLLK1809 KWALYSFNDG1819 EEHQKILLDD1829 LMKKAEEGDL 1839 LVNPDQPRLT1849 IPISQIAPDL1859 ILADLPRNIM1869 LNNDELEFEQ1879 APEFLLGDGS 1889 FGSVYRAAYE1899 GEEVAVKIFN1909 KHTSLRLLRQ1919 ELVVLCHLHH1929 PSLISLLAAG 1939 IRPRMLVMEL1949 ASKGSLDRLL1959 QQDKASLTRT1969 LQHRIALHVA1979 DGLRYLHSAM 1989 IIYRDLKPHN1999 VLLFTLYPNA2009 AIIAKIADYG2019 IAQYCCRMTS2032 EGTPGFRAPE 2042 VARGNVIYNQ2052 QADVYSFGLL2062 LYDILTTGGR2072 IVEGLKFPNE2082 FDELEIQGKL 2092 PDPVKEYGCA2102 PWPMVEKLIK2112 QCLKENPQER2122 PTSAQVFDIL2132 NSAELVCLTR 2142 RILLPKNVIV2152 ECMVATHHNS2162 RNASIWLGCG2172 HTDRGQLSFL2182 DLNTEGYTSE 2192 EVADSRILCL2202 ALVHLPVEKE2212 SWIVSGTQSG2222 TLLVINTEDG2232 KKRHTLEKMT 2242 DSVTCLYCNS2252 FSKQSKQKNF2262 LLVGTADGKL2272 AIFEDKTVKL2282 KGAAPLKILN 2292 IGNVSTPLMC2302 LSESTNSTER2312 NVMWGGCGTK2322 IFSFSNDFTI2332 QKLIETRTSQ 2342 LFSYAAFSDS2352 NIITVVVDTA2362 LYIAKQNSPV2372 VEVWDKKTEK2382 LCGLIDCVHF 2392 LREVTVKENK2402 ESKHKMSYSG2412 RVKTLCLQKN2422 TALWIGTGGG2432 HILLLDLSTR 2442 RLIRVIYNFC2452 NSVRVMMTAQ2462 LGSLKNVMLV2472 LGYNRKNTEG2482 TQKQKEIQSC 2492 LTVWDINLPH2502 EVQNLEKHIE2512 VRKELAEKMR2522 RTSVE
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Phosphonothreonine | Ligand Info | |||||
| Structure Description | Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2) | PDB:6VP6 | ||||
| Method | Electron microscopy | Resolution | 3.47 Å | Mutation | No | [10] |
| PDB Sequence |
VPYNRMKLMI
1339 VGNGSGKTTL1350 LQQLMGIDVK1374 DWPILVLNVW1393 DFAGREEFYS1403 THPRALYLAV 1418 YDLSKGQAEV1428 DAMKPWLFNI1438 KARASSSPVI1448 LVGTHLDVSD1458 EKQRKACMSK 1468 ITKELLNKRG1478 FPAIRDYHFV1488 NATEESDALA1498 KLRKTIINES1508 LNFKIRDQLV 1518 VGQLIPDCYV1528 ELEKIILSER1538 KNVPIEFPVI1548 DRKRLLQLVR1558 ENQLQLDENE 1568 LPHAVHFLNE1578 SGVLLHFQAL1590 QLSDLYFVEP1600 KWLCKIMAQI1610 LTVGIISRRD 1630 VEKFLSKKRK1640 FPKNYMSQYF1650 KLLEKFQIAL1660 PIGEEYLLVP1670 SSLSDHRPVI 1680 ELPHCENSEI1690 IIRLYEMPYF1700 PMGFWSRLIN1710 RLLEISPYML1720 LRPNRMYWRQ 1736 GIYLNWSPEA1746 YCLVGSEVLD1756 NHPESFLKIT1766 VPSCRKGCIL1776 LGQVVDHIDS 1786 LMEEWFPGLL1796 LLKKWALYSF1816 NDGEEHQKIL1826 LDDLMKKAEE1836 GDLLVNPDQP 1846 RLTIPISQIA1856 PDLILADLPR1866 NIMLNNDELE1876 FEQAPEFLLG1886 DGSFGSVYRA 1896 AYEGEEVAVK1906 IFNKHTSLRL1916 LRQELVVLCH1926 LHHPSLISLL1936 AAGIRPRMLV 1946 MELASKGSLD1956 RLLQQDKASL1966 TRTLQHRIAL1976 HVADGLRYLH1986 SAMIIYRDLK 1996 PHNVLLFTLY2006 PNAAIIAKIA2016 DYGPGFRAPE2042 VARGNVIYNQ2052 QADVYSFGLL 2062 LYDILTTGGR2072 IVEGLKFPNE2082 FDELEIQGKL2092 PDPVKEYGCA2102 PWPMVEKLIK 2112 QCLKENPQER2122 PTSAQVFDIL2132 NSAELVCLTR2142 RILLPKNVIV2152 ECMVATHHAS 2166 IWLGCGHTDR2176 GQLSFLDLNT2186 EGYTSEEVAD2196 SRILCLALVH2206 LPVEKESWIV 2216 SGTQSGTLLV2226 INTEDGKKRH2236 TLEKMTDSVT2246 CLYCNFLLVG2266 TADGKLAIFE 2276 DKTVKLKGAA2286 PLKILNIGNV2296 STPLMCLSES2306 NVMWGGCGTK2322 IFSFSNDFTI 2332 QKLIETRTSQ2342 LFSYAAFSDS2352 NIITVVVDTA2362 LYIAKQNSPV2372 VEVWDKKTEK 2382 LCGLIDCVHF2392 LREVMMSYSG2412 RVKTLCLQKN2422 TALWIGTGGG2432 HILLLDLSTR 2442 RLIRVIYNFC2452 NSVRVMMTAQ2462 LGSLKNVMLV2472 LGYNREIQSC2492 LTVWDINLPH 2502 EVQNLEKHIE2512 VRKELAEKMR2522 RTS
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Click to View More Binding Site Information of This Target with Different Ligands | ||||||
| Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Tissue Distribution
of target is determined from a proteomics study that quantified more than 12,000 genes across 32 normal human tissues. Tissue Specificity (TS) score was used to define the enrichment of target across tissues.
The distribution of targets among different tissues or organs need to be taken into consideration when assessing the target druggability, as it is generally accepted that the wider the target distribution, the greater the concern over potential adverse effects
(Nat Rev Drug Discov, 20: 64-81, 2021).
Biological Network Descriptors
of target is determined based on a human protein-protein interactions (PPI) network consisting of 9,309 proteins and 52,713 PPIs, which were with a high confidence score of ≥ 0.95 collected from STRING database.
The network properties of targets based on protein-protein interactions (PPIs) have been widely adopted for the assessment of target’s druggability. Proteins with high node degree tend to have a high impact on network function through multiple interactions, while proteins with high betweenness centrality are regarded to be central for communication in interaction networks and regulate the flow of signaling information
(Front Pharmacol, 9, 1245, 2018;
Curr Opin Struct Biol. 44:134-142, 2017).
Human Similarity Proteins
Human Tissue Distribution
Biological Network Descriptors
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Note:
If a protein has TS (tissue specficity) scores at least in one tissue >= 2.5, this protein is called tissue-enriched (including tissue-enriched-but-not-specific and tissue-specific). In the plots, the vertical lines are at thresholds 2.5 and 4.
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| Degree | 22 | Degree centrality | 2.36E-03 | Betweenness centrality | 5.31E-03 |
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| Closeness centrality | 2.47E-01 | Radiality | 1.43E+01 | Clustering coefficient | 6.93E-02 |
| Neighborhood connectivity | 3.56E+01 | Topological coefficient | 5.68E-02 | Eccentricity | 11 |
| Download | Click to Download the Full PPI Network of This Target | ||||
| Chemical Structure based Activity Landscape of Target | Top |
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| Drug Property Profile of Target | Top | |
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| (1) Molecular Weight (mw) based Drug Clustering | (2) Octanol/Water Partition Coefficient (xlogp) based Drug Clustering | |
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| (3) Hydrogen Bond Donor Count (hbonddonor) based Drug Clustering | (4) Hydrogen Bond Acceptor Count (hbondacc) based Drug Clustering | |
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| (5) Rotatable Bond Count (rotbonds) based Drug Clustering | (6) Topological Polar Surface Area (polararea) based Drug Clustering | |
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| "RO5" indicates the cutoff set by lipinski's rule of five; "D123AB" colored in GREEN denotes the no violation of any cutoff in lipinski's rule of five; "D123AB" colored in PURPLE refers to the violation of only one cutoff in lipinski's rule of five; "D123AB" colored in BLACK represents the violation of more than one cutoffs in lipinski's rule of five | ||
| Target Poor or Non Binders | Top | |||||
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| Target Poor or Non Binders | ||||||
| Target Regulators | Top | |||||
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| Target-regulating microRNAs | ||||||
| Target-interacting Proteins | ||||||
| References | Top | |||||
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| REF 1 | Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA) | |||||
| REF 2 | ClinicalTrials.gov (NCT03976349) A Phase 1 Single- and Multiple-Ascending-Dose Study to Assess the Safety, Tolerability, and Pharmacokinetics of BIIB094 Administered Intrathecally to Adults With Parkinson's Disease. U.S.National Institutes of Health. | |||||
| REF 3 | Clinical pipeline report, company report or official report of Ionis | |||||
| REF 4 | Leucine-rich repeat kinase 2 inhibitors: a patent review (2014-2016).Expert Opin Ther Pat. 2017 Jun;27(6):667-676. | |||||
| REF 5 | Discovery of highly potent, selective, and brain-penetrant aminopyrazole leucine-rich repeat kinase 2 (LRRK2) small molecule inhibitors. J Med Chem. 2014 Feb 13;57(3):921-36. | |||||
| REF 6 | URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2059). | |||||
| REF 7 | Discovery and preclinical profiling of 3-[4-(morpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-5-yl]benzonitrile (PF-06447475), a highly potent, selective, brain penetrant, and in vivo active LRRK2 kinase inhibitor. J Med Chem. 2015 Jan 8;58(1):419-32. | |||||
| REF 8 | Discovery, synthesis, and characterization of an orally bioavailable, brain penetrant inhibitor of mixed lineage kinase 3. J Med Chem. 2013 Oct 24;56(20):8032-48. | |||||
| REF 9 | Structural analysis of the full-length human LRRK2. Cell. 2021 Jun 24;184(13):3519-3527.e10. | |||||
| REF 10 | Structure of LRRK2 in Parkinson's disease and model for microtubule interaction. Nature. 2020 Dec;588(7837):344-349. | |||||
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