Binding Site Information of Target
Target General Information | Top | ||||
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Target ID | T72849 | Target Info | |||
Target Name | Adipocyte-derived leucine aminopeptidase (ERAP1) | ||||
Synonyms | Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; ERAP1; Aminopeptidase PILS; ARTS-1; ALAP; A-LAP | ||||
Target Type | Literature-reported Target | ||||
Gene Name | ERAP1 | ||||
Biochemical Class | Peptidase | ||||
UniProt ID |
Drug Binding Sites of Target | Top | |||||
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Ligand Name: Bestatin | Ligand Info | |||||
Structure Description | Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1 | PDB:2YD0 | ||||
Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [1] |
PDB Sequence |
PFPWNKIRLP
55 EYVIPVHYDL65 LIHANLTTLT75 FWGTTKVEIT85 ASQPTSTIIL95 HSHHLQISRA 105 TLRKGLSEEP119 LQVLEHPRQE129 QIALLAPEPL139 LVGLPYTVVI149 HYAGNLSETF 159 HGFYKSTYRT169 KEGELRILAS179 TQFEPTAARM189 AFPCFDEPAF199 KASFSIKIRR 209 EPRHLAISNM219 PLVKSVTVAE229 GLIEDHFDVT239 VKMSTYLVAF249 IISDFESVSK 259 ITKSGVKVSV269 YAVPDKINQA279 DYALDAAVTL289 LEFYEDYFSI299 PYPLPKQDLA 309 AIPDFQSGAM319 ENWGLTTYRE329 SALLFDAEKS339 SASSKLGITM349 TVAHELAHQW 359 FGNLVTMEWW369 NDLWLNEGFA379 KFMEFVSVSV389 THPELKVGDY399 FFGKCFDAME 409 VDALNSSHPV419 STPVENPAQI429 REMFDDVSYD439 KGACILNMLR449 EYLSADAFKS 459 GIVQYLQKHS469 YKNTKNEDLW479 DSMASIGVDV517 KTMMNTWTLQ527 KGFPLITITV 537 RGRNVHMKQE547 HYMKGDTGYL562 WHVPLTFITS572 KSDMVHRFLL582 KTKTDVLILP 592 EEVEWIKFNV602 GMNGYYIVHY612 EDDGWDSLTG622 LLKGTHTAVS632 SNDRASLINN 642 AFQLVSIGKL652 SIEKALDLSL662 YLKHETEIMP672 VFQGLNELIP682 MYKLMEKRDM 692 NEVETQFKAF702 LIRLLRDLID712 KQTWTDEGSV722 SERMLRSQLL732 LLACVHNYQP 742 CVQRAEGYFR752 KWKESNGNLS762 LPVDVTLAVF772 AVGAQSTEGW782 DFLYSKYQFS 792 LSSTEKSQIE802 FALCRTQNKE812 KLQWLLDESF822 KGDKIKTQEF832 PQILTLIGRN 842 PVGYPLAWQF852 LRKNWNKLVQ862 KFELGSSSIA872 HMVMGTTNQF882 STRTRLEEVK 892 GFFSSLKENG902 SQLRCVQQTI912 ETIEENIGWM922 DKNFDKIRVW932 LQSEKLER |
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Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
Ligand Name: Propanoic acid | Ligand Info | |||||
Structure Description | High-resolution crystal structure of ERAP1 in complex with 15mer phosphinic peptide | PDB:6RYF | ||||
Method | X-ray diffraction | Resolution | 1.72 Å | Mutation | No | [2] |
PDB Sequence |
PFPWNKIRLP
55 EYVIPVHYDL65 LIHANLTTLT75 FWGTTKVEIT85 ASQPTSTIIL95 HSHHLQISRA 105 TLRKRLSEEP119 LQVLEHPRQE129 QIALLAPEPL139 LVGLPYTVVI149 HYAGNLSETF 159 HGFYKSTYRT169 KEGELRILAS179 TQFEPTAARM189 AFPCFDEPAF199 KASFSIKIRR 209 EPRHLAISNM219 PLVKSVTVAE229 GLIEDHFDVT239 VKMSTYLVAF249 IISDFESVSK 259 ITKSGVKVSV269 YAVPDKINQA279 DYALDAAVTL289 LEFYEDYFSI299 PYPLPKQDLA 309 AIPDFQSGAM319 ENWGLTTYRE329 SALLFDAEKS339 SASSKLGITM349 TVAHELAHQW 359 FGNLVTMEWW369 NDLWLNEGFA379 KFMEFVSVSV389 THPELKVGDY399 FFGKCFDAME 409 VDALNSSHPV419 STPVENPAQI429 REMFDDVSYD439 KGACILNMLR449 EYLSADAFKS 459 GIVQYLQKHS469 YKNTKNEDLW479 DSMASIVDVK518 TMMNTWTLQK528 GFPLITITVR 538 GRNVHMKQEH548 YMKGDTGYLW563 HVPLTFITSK573 SDMVHRFLLK583 TKTDVLILPE 593 EVEWIKFNVG603 MNGYYIVHYE613 DDGWDSLTGL623 LKGTHTAVSS633 NDRASLINNA 643 FQLVSIGKLS653 IEKALDLSLY663 LKHETEIMPV673 FQGLNELIPM683 YKLMEKRDMN 693 EVETQFKAFL703 IRLLRDLIDK713 QTWTDEGSVS723 ERMLRSQLLL733 LACVHNYQPC 743 VQRAEGYFRK753 WKESNGNLSL763 PVDVTLAVFA773 VGAQSTEGWD783 FLYSKYQFSL 793 SSTEKSQIEF803 ALCRTQNKEK813 LQWLLDESFK823 GDKIKTQEFP833 QILTLIGRNP 843 VGYPLAWQFL853 RKNWNKLVQK863 FELGSSSIAH873 MVMGTTNQFS883 TRTRLEEVKG 893 FFSSLKENGS903 QLRCVQQTIE913 TIEENIGWMD923 KNFDKIRVWL933 QSEKLR |
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Ligand Name: (4~{a}~{R},5~{S},6~{R},8~{S},8~{a}~{R})-5-[2-(furan-3-yl)ethyl]-5,6,8~{a}-trimethyl-8-oxidanyl-3,4,4~{a},6,7,8-hexahydronaphthalene-1-carboxylic acid | Ligand Info | |||||
Structure Description | Human endoplasmic reticulum aminopeptidase 1 (ERAP1) in complex with (4aR,5S,6R,8S,8aR)-5-(2-(Furan-3-yl)ethyl)-8-hydroxy-5,6,8a-trimethyl-3,4,4a,5,6,7,8,8a-octahydronaphthalene-1-carboxylic acid | PDB:6T6R | ||||
Method | X-ray diffraction | Resolution | 1.67 Å | Mutation | Yes | [3] |
PDB Sequence |
TPFPWNKIRL
54 PEYVIPVHYD64 LLIHAQLTTL74 TFWGTTKVEI84 TASQPTSTII94 LHSHHLQISR 104 ATLRKGAGER114 LSEEPLQVLE124 HPRQEQIALL134 APEPLLVGLP144 YTVVIHYAGQ 154 LSETFHGFYK164 STYRTKEGEL174 RILASTQFEP184 TAARMAFPCF194 DEPAFKASFS 204 IKIRREPRHL214 AISNMPLVKS224 VTVAEGLIED234 HFDVTVKMST244 YLVAFIISDF 254 ESVSKITKSG264 VKVSVYAVPD274 KINQADYALD284 AAVTLLEFYE294 DYFSIPYPLP 304 KQDLAAIPDF314 QSGAMENWGL324 TTYRESALLF334 DAEKSSASSK344 LGITMTVAHE 354 LAHQWFGNLV364 TMEWWNDLWL374 NEGFAKFMEF384 VSVSVTHPEL394 KVGDYFFGKC 404 FDAMEVDALQ414 SSHPVSTPVE424 NPAQIREMFD434 DVSYDKGACI444 LNMLREYLSA 454 DAFKSGIVQY464 LQKHSYKNTK474 NEDLWDSMAS484 IGVDVKTMMN522 TWTLQKGFPL 532 ITITVRGRNV542 HMKQEHYMKG552 GYLWHVPLTF569 ITSKSDMVHR579 FLLKTKTDVL 589 ILPEEVEWIK599 FNVGMNGYYI609 VHYEDDGWDS619 LTGLLKGTHT629 AVSSNDRASL 639 INNAFQLVSI649 GKLSIEKALD659 LSLYLKHETE669 IMPVFQGLNE679 LIPMYKLMEK 689 RDMNEVETQF699 KAFLIRLLRD709 LIDKQTWTDE719 GSVSERMLRS729 QLLLLACVHN 739 YQPCVQRAEG749 YFRKWKESNG759 QLSLPVDVTL769 AVFAVGAQST779 EGWDFLYSKY 789 QFSLSSTEKS799 QIEFALCRTQ809 NKEKLQWLLD819 ESFKGDKIKT829 QEFPQILTLI 839 GRNPVGYPLA849 WQFLRKNWNK859 LVQKFELGSS869 SIAHMVMGTT879 NQFSTRTRLE 889 EVKGFFSSLK899 ENGSQLRCVQ909 QTIETIEENI919 GWMDKNFDKI929 RVWLQS |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MNZ or .MNZ2 or .MNZ3 or :3MNZ;style chemicals stick;color identity;select .A:674 or .A:677 or .A:678 or .A:681 or .A:684 or .A:685 or .A:688 or .A:730 or .A:733 or .A:734 or .A:737 or .A:738 or .A:803 or .A:807 or .A:841; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: [(1~{R})-1-[[(2~{S})-2-[[(2~{S})-1-azaniumyl-1-oxidanylidene-3-phenyl-propan-2-yl]carbamoyl]pent-4-ynyl]-oxidanyl-phosphoryl]-3-phenyl-propyl]azanium | Ligand Info | |||||
Structure Description | High-resolution crystal structure of ERAP1 with bound phosphinic transition-state analogue inhibitor | PDB:6Q4R | ||||
Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | No | [4] |
PDB Sequence |
TPFPWNKIRL
54 PEYVIPVHYD64 LLIHANLTTL74 TFWGTTKVEI84 TASQPTSTII94 LHSHHLQISR 104 ATLRKRLSEE118 PLQVLEHPRQ128 EQIALLAPEP138 LLVGLPYTVV148 IHYAGNLSET 158 FHGFYKSTYR168 TKEGELRILA178 STQFEPTAAR188 MAFPCFDEPA198 FKASFSIKIR 208 REPRHLAISN218 MPLVKSVTVA228 EGLIEDHFDV238 TVKMSTYLVA248 FIISDFESVS 258 KITKSGVKVS268 VYAVPDKINQ278 ADYALDAAVT288 LLEFYEDYFS298 IPYPLPKQDL 308 AAIPDFQSGA318 MENWGLTTYR328 ESALLFDAEK338 SSASSKLGIT348 MTVAHELAHQ 358 WFGNLVTMEW368 WNDLWLNEGF378 AKFMEFVSVS388 VTHPELKVGD398 YFFGKCFDAM 408 EVDALNSSHP418 VSTPVENPAQ428 IREMFDDVSY438 DKGACILNML448 REYLSADAFK 458 SGIVQYLQKH468 SYKNTKNEDL478 WDSMASIVDV517 KTMMNTWTLQ527 KGFPLITITV 537 RGRNVHMKQE547 HYMKGDTGYL562 WHVPLTFITS572 KSDMVHRFLL582 KTKTDVLILP 592 EEVEWIKFNV602 GMNGYYIVHY612 EDDGWDSLTG622 LLKGTHTAVS632 SNDRASLINN 642 AFQLVSIGKL652 SIEKALDLSL662 YLKHETEIMP672 VFQGLNELIP682 MYKLMEKRDM 692 NEVETQFKAF702 LIRLLRDLID712 KQTWTDEGSV722 SERMLRSQLL732 LLACVHNYQP 742 CVQRAEGYFR752 KWKESNGNLS762 LPVDVTLAVF772 AVGAQSTEGW782 DFLYSKYQFS 792 LSSTEKSQIE802 FALCRTQNKE812 KLQWLLDESF822 KGDKIKTQEF832 PQILTLIGRN 842 PVGYPLAWQF852 LRKNWNKLVQ862 KFELGSSSIA872 HMVMGTTNQF882 STRTRLEEVK 892 GFFSSLKENG902 SQLRCVQQTI912 ETIEENIGWM922 DKNFDKIRVW932 LQSEK |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .HJ5 or .HJ52 or .HJ53 or :3HJ5;style chemicals stick;color identity;select .A:181 or .A:183 or .A:184 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320 or .A:349 or .A:350 or .A:353 or .A:354 or .A:357 or .A:376 or .A:380 or .A:383 or .A:430 or .A:433 or .A:438 or .A:868 or .A:869 or .A:870; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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GLN181
3.171
GLU183
1.986
PRO184
3.776
GLN315
3.957
SER316
2.603
GLY317
2.680
ALA318
2.306
MET319
2.954
GLU320
1.906
MET349
4.116
THR350
3.814
HIS353
2.984
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Ligand Name: [(1~{R})-1-azanyl-3-phenyl-propyl]-[(2~{S})-2-methanoyl-4-methyl-pentyl]phosphinic acid | Ligand Info | |||||
Structure Description | High-resolution crystal structure of ERAP1 in complex with 15mer phosphinic peptide | PDB:6RYF | ||||
Method | X-ray diffraction | Resolution | 1.72 Å | Mutation | No | [2] |
PDB Sequence |
PFPWNKIRLP
55 EYVIPVHYDL65 LIHANLTTLT75 FWGTTKVEIT85 ASQPTSTIIL95 HSHHLQISRA 105 TLRKRLSEEP119 LQVLEHPRQE129 QIALLAPEPL139 LVGLPYTVVI149 HYAGNLSETF 159 HGFYKSTYRT169 KEGELRILAS179 TQFEPTAARM189 AFPCFDEPAF199 KASFSIKIRR 209 EPRHLAISNM219 PLVKSVTVAE229 GLIEDHFDVT239 VKMSTYLVAF249 IISDFESVSK 259 ITKSGVKVSV269 YAVPDKINQA279 DYALDAAVTL289 LEFYEDYFSI299 PYPLPKQDLA 309 AIPDFQSGAM319 ENWGLTTYRE329 SALLFDAEKS339 SASSKLGITM349 TVAHELAHQW 359 FGNLVTMEWW369 NDLWLNEGFA379 KFMEFVSVSV389 THPELKVGDY399 FFGKCFDAME 409 VDALNSSHPV419 STPVENPAQI429 REMFDDVSYD439 KGACILNMLR449 EYLSADAFKS 459 GIVQYLQKHS469 YKNTKNEDLW479 DSMASIVDVK518 TMMNTWTLQK528 GFPLITITVR 538 GRNVHMKQEH548 YMKGDTGYLW563 HVPLTFITSK573 SDMVHRFLLK583 TKTDVLILPE 593 EVEWIKFNVG603 MNGYYIVHYE613 DDGWDSLTGL623 LKGTHTAVSS633 NDRASLINNA 643 FQLVSIGKLS653 IEKALDLSLY663 LKHETEIMPV673 FQGLNELIPM683 YKLMEKRDMN 693 EVETQFKAFL703 IRLLRDLIDK713 QTWTDEGSVS723 ERMLRSQLLL733 LACVHNYQPC 743 VQRAEGYFRK753 WKESNGNLSL763 PVDVTLAVFA773 VGAQSTEGWD783 FLYSKYQFSL 793 SSTEKSQIEF803 ALCRTQNKEK813 LQWLLDESFK823 GDKIKTQEFP833 QILTLIGRNP 843 VGYPLAWQFL853 RKNWNKLVQK863 FELGSSSIAH873 MVMGTTNQFS883 TRTRLEEVKG 893 FFSSLKENGS903 QLRCVQQTIE913 TIEENIGWMD923 KNFDKIRVWL933 QSEKLR |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KF2 or .KF22 or .KF23 or :3KF2;style chemicals stick;color identity;select .A:181 or .A:183 or .A:184 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320 or .A:350 or .A:353 or .A:354 or .A:357 or .A:376 or .A:380 or .A:383 or .A:433 or .A:438; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Ligand Name: D-malate | Ligand Info | |||||
Structure Description | High-resolution crystal structure of ERAP1 with bound bestatin analogue inhibitor | PDB:7Z28 | ||||
Method | X-ray diffraction | Resolution | 1.55 Å | Mutation | No | [5] |
PDB Sequence |
TPFPWNKIRL
54 PEYVIPVHYD64 LLIHANLTTL74 TFWGTTKVEI84 TASQPTSTII94 LHSHHLQISR 104 ATLRKGAGER114 LSEEPLQVLE124 HPRQEQIALL134 APEPLLVGLP144 YTVVIHYAGN 154 LSETFHGFYK164 STYRTKEGEL174 RILASTQFEP184 TAARMAFPCF194 DEPAFKASFS 204 IKIRREPRHL214 AISNMPLVKS224 VTVAEGLIED234 HFDVTVKMST244 YLVAFIISDF 254 ESVSKITKSG264 VKVSVYAVPD274 KINQADYALD284 AAVTLLEFYE294 DYFSIPYPLP 304 KQDLAAIPDF314 QSGAMENWGL324 TTYRESALLF334 DAEKSSASSK344 LGITMTVAHE 354 LAHQWFGNLV364 TMEWWNDLWL374 NEGFAKFMEF384 VSVSVTHPEL394 KVGDYFFGKC 404 FDAMEVDALN414 SSHPVSTPVE424 NPAQIREMFD434 DVSYDKGACI444 LNMLREYLSA 454 DAFKSGIVQY464 LQKHSYKNTK474 NEDLWDSMAS484 ISGDVKTMMN522 TWTLQKGFPL 532 ITITVRGRNV542 HMKQEHYMKG552 DTGYLWHVPL567 TFITSKSDMV577 HRFLLKTKTD 587 VLILPEEVEW597 IKFNVGMNGY607 YIVHYEDDGW617 DSLTGLLKGT627 HTAVSSNDRA 637 SLINNAFQLV647 SIGKLSIEKA657 LDLSLYLKHE667 TEIMPVFQGL677 NELIPMYKLM 687 EKRDMNEVET697 QFKAFLIRLL707 RDLIDKQTWT717 DEGSVSERML727 RSQLLLLACV 737 HNYQPCVQRA747 EGYFRKWKES757 NGNLSLPVDV767 TLAVFAVGAQ777 STEGWDFLYS 787 KYQFSLSSTE797 KSQIEFALCR807 TQNKEKLQWL817 LDESFKGDKI827 KTQEFPQILT 837 LIGRNPVGYP847 LAWQFLRKNW857 NKLVQKFELG867 SSSIAHMVMG877 TTNQFSTRTR 887 LEEVKGFFSS897 LKENGSQLRC907 VQQTIETIEE917 NIGWMDKNFD927 KIRVWLQSE |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MLT or .MLT2 or .MLT3 or :3MLT;style chemicals stick;color identity;select .A:681 or .A:684 or .A:685 or .A:688 or .A:730 or .A:733 or .A:734 or .A:737 or .A:738 or .A:803 or .A:841; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
Ligand Name: methyl (2~{S})-2-[[(2~{S})-2-[[(2~{S},3~{R})-3-azanyl-2,7-bis(oxidanyl)heptanoyl]amino]-4-methyl-pentanoyl]amino]-3-(4-hydroxyphenyl)propanoate | Ligand Info | |||||
Structure Description | High-resolution crystal structure of ERAP1 with bound bestatin analogue inhibitor | PDB:7Z28 | ||||
Method | X-ray diffraction | Resolution | 1.55 Å | Mutation | No | [5] |
PDB Sequence |
TPFPWNKIRL
54 PEYVIPVHYD64 LLIHANLTTL74 TFWGTTKVEI84 TASQPTSTII94 LHSHHLQISR 104 ATLRKGAGER114 LSEEPLQVLE124 HPRQEQIALL134 APEPLLVGLP144 YTVVIHYAGN 154 LSETFHGFYK164 STYRTKEGEL174 RILASTQFEP184 TAARMAFPCF194 DEPAFKASFS 204 IKIRREPRHL214 AISNMPLVKS224 VTVAEGLIED234 HFDVTVKMST244 YLVAFIISDF 254 ESVSKITKSG264 VKVSVYAVPD274 KINQADYALD284 AAVTLLEFYE294 DYFSIPYPLP 304 KQDLAAIPDF314 QSGAMENWGL324 TTYRESALLF334 DAEKSSASSK344 LGITMTVAHE 354 LAHQWFGNLV364 TMEWWNDLWL374 NEGFAKFMEF384 VSVSVTHPEL394 KVGDYFFGKC 404 FDAMEVDALN414 SSHPVSTPVE424 NPAQIREMFD434 DVSYDKGACI444 LNMLREYLSA 454 DAFKSGIVQY464 LQKHSYKNTK474 NEDLWDSMAS484 ISGDVKTMMN522 TWTLQKGFPL 532 ITITVRGRNV542 HMKQEHYMKG552 DTGYLWHVPL567 TFITSKSDMV577 HRFLLKTKTD 587 VLILPEEVEW597 IKFNVGMNGY607 YIVHYEDDGW617 DSLTGLLKGT627 HTAVSSNDRA 637 SLINNAFQLV647 SIGKLSIEKA657 LDLSLYLKHE667 TEIMPVFQGL677 NELIPMYKLM 687 EKRDMNEVET697 QFKAFLIRLL707 RDLIDKQTWT717 DEGSVSERML727 RSQLLLLACV 737 HNYQPCVQRA747 EGYFRKWKES757 NGNLSLPVDV767 TLAVFAVGAQ777 STEGWDFLYS 787 KYQFSLSSTE797 KSQIEFALCR807 TQNKEKLQWL817 LDESFKGDKI827 KTQEFPQILT 837 LIGRNPVGYP847 LAWQFLRKNW857 NKLVQKFELG867 SSSIAHMVMG877 TTNQFSTRTR 887 LEEVKGFFSS897 LKENGSQLRC907 VQQTIETIEE917 NIGWMDKNFD927 KIRVWLQSE |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .I88 or .I882 or .I883 or :3I88;style chemicals stick;color identity;select .A:181 or .A:183 or .A:184 or .A:315 or .A:316 or .A:317 or .A:318 or .A:319 or .A:320 or .A:328 or .A:349 or .A:350 or .A:353 or .A:354 or .A:357 or .A:376 or .A:380 or .A:383 or .A:433 or .A:438 or .A:833 or .A:869 or .A:870 or .A:873; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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GLN181
3.759
GLU183
2.760
PRO184
4.083
GLN315
3.898
SER316
2.921
GLY317
2.410
ALA318
3.158
MET319
3.739
GLU320
2.631
ARG328
3.581
MET349
4.719
THR350
3.688
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References | Top | ||||
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REF 1 | Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming. Proc Natl Acad Sci U S A. 2011 May 10;108(19):7745-50. | ||||
REF 2 | Mechanism for antigenic peptide selection by endoplasmic reticulum aminopeptidase 1. Proc Natl Acad Sci U S A. 2019 Dec 26;116(52):26709-26716. | ||||
REF 3 | Targeting the Regulatory Site of ER Aminopeptidase 1 Leads to the Discovery of a Natural Product Modulator of Antigen Presentation. J Med Chem. 2020 Mar 26;63(6):3348-3358. | ||||
REF 4 | High-Resolution Crystal Structure of Endoplasmic Reticulum Aminopeptidase 1 with Bound Phosphinic Transition-State Analogue Inhibitor. ACS Med Chem Lett. 2019 Feb 13;10(5):708-713. | ||||
REF 5 | Discovery of Selective Nanomolar Inhibitors for Insulin-Regulated Aminopeptidase Based on Alpha-Hydroxy-beta-amino Acid Derivatives of Bestatin. J Med Chem. 2022 Jul 28;65(14):10098-10117. |
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