eF-site ID 1fv1-ABCDEF PDB Code 1fv1 Chain A, B, C, D, E, F click to enlarge Title STRUCTURAL BASIS FOR THE BINDING OF AN IMMUNODOMINANT PEPTIDE FROM MYELIN BASIC PROTEIN IN DIFFERENT REGISTERS BY TWO HLA-DR2 ALLELES Classification IMMUNE SYSTEM Compound MAJOR HISTOCOMPATIBILITY COMPLEX ALPHA CHAIN Source Homo sapiens (Human) (MBP_HUMAN) Sequence A:  EEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETV WRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPI TNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWL RNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYD CRVEHWGLDEPLLKHWEFD B:  GDTRPRFLQQDKYECHFFNGTERVRFLHRDIYNQEEDLRF DSDVGEYRAVTELGRPDAEYWNSQKDFLEDRRAAVDTYCR HNYGVGESFTVQRRVEPKVTVYPARTQTLQHHNLLVCSVN GFYPGSIEVRWFRNSQEEKAGVVSTGLIQNGDWTFQTLVM LETVPRSGEVYTCQVEHPSVTSPLTVEWRA C:  NPVVHFFKNIVTPRTPPPSQ D:  EHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVW RLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPIT NVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLR NGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDC RVEHWGLDEPLLKHWEFD E:  GDTRPRFLQQDKYECHFFNGTERVRFLHRDIYNQEEDLRF DSDVGEYRAVTELGRPDAEYWNSQKDFLEDRRAAVDTYCR HNYGVGESFTVQRRVEPKVTVYPARTQTLQHHNLLVCSVN GFYPGSIEVRWFRNSQEEKAGVVSTGLIQNGDWTFQTLVM LETVPRSGEVYTCQVEHPSVTSPLTVEWRA F:  PVVHFFKNIVTPRTPPPS Description (1)  MAJOR HISTOCOMPATIBILITY COMPLEX ALPHA CHAIN/MAJOR HISTOCOMPATIBILITY COMPLEX BETA CHAIN/MYELIN BASIC PROTEIN Functional site 1) chain D residue 123 type sequence R description BINDING SITE FOR RESIDUE SO4 D 182 source : AC1 2) chain D residue 124 type sequence N description BINDING SITE FOR RESIDUE SO4 D 182 source : AC1 3) chain D residue 126 type sequence K description BINDING SITE FOR RESIDUE SO4 D 182 source : AC1 4) chain A residue 123 type sequence R description BINDING SITE FOR RESIDUE SO4 A 182 source : AC2 5) chain A residue 124 type sequence N description BINDING SITE FOR RESIDUE SO4 A 182 source : AC2 6) chain A residue 126 type sequence K description BINDING SITE FOR RESIDUE SO4 A 182 source : AC2 7) chain B residue 29 type sequence R description BINDING SITE FOR RESIDUE SO4 B 191 source : AC3 8) chain B residue 39 type sequence R description BINDING SITE FOR RESIDUE SO4 B 191 source : AC3 9) chain E residue 29 type sequence R description BINDING SITE FOR RESIDUE SO4 B 191 source : AC3 10) chain E residue 39 type sequence R description BINDING SITE FOR RESIDUE SO4 B 191 source : AC3 11) chain B residue 48 type sequence R description BINDING SITE FOR RESIDUE GOL D 183 source : AC4 12) chain D residue 110 type sequence D description BINDING SITE FOR RESIDUE GOL D 183 source : AC4 13) chain D residue 111 type sequence K description BINDING SITE FOR RESIDUE GOL D 183 source : AC4 14) chain D residue 140 type sequence R description BINDING SITE FOR RESIDUE GOL D 183 source : AC4 15) chain B residue 94 type sequence R description BINDING SITE FOR RESIDUE GOL B 192 source : AC5 16) chain B residue 179 type sequence S description BINDING SITE FOR RESIDUE GOL B 192 source : AC5 17) chain D residue 67 type sequence K description BINDING SITE FOR RESIDUE GOL B 192 source : AC5 18) chain D residue 71 type sequence E description BINDING SITE FOR RESIDUE GOL B 192 source : AC5 19) chain C residue 100 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P02687 source Swiss-Prot : SWS_FT_FI4 20) chain F residue 100 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P02687 source Swiss-Prot : SWS_FT_FI4 21) chain C residue 92 type SITE sequence F description Cleavage; by CTSG => ECO:0000269|PubMed:15100291 source Swiss-Prot : SWS_FT_FI1 22) chain F residue 92 type SITE sequence F description Cleavage; by CTSG => ECO:0000269|PubMed:15100291 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 97 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P02688 source Swiss-Prot : SWS_FT_FI2 24) chain F residue 97 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P02688 source Swiss-Prot : SWS_FT_FI2 25) chain D residue 49 type MOD_RES sequence G description Phosphothreonine => ECO:0000250|UniProtKB:P02688 source Swiss-Prot : SWS_FT_FI2 26) chain D residue 52 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:P02688 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 99 type MOD_RES sequence R description Citrulline => ECO:0000269|PubMed:23828821 source Swiss-Prot : SWS_FT_FI3 28) chain F residue 99 type MOD_RES sequence R description Citrulline => ECO:0000269|PubMed:23828821 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 105 type MOD_RES sequence Q description Deamidated glutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 62 type SITE sequence N description Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4GBX source Swiss-Prot : SWS_FT_FI6 31) chain D residue 62 type SITE sequence N description Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4GBX source Swiss-Prot : SWS_FT_FI6 32) chain A residue 69 type SITE sequence N description Pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX source Swiss-Prot : SWS_FT_FI7 33) chain D residue 69 type SITE sequence N description Pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:21115828, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX source Swiss-Prot : SWS_FT_FI7 34) chain A residue 76 type SITE sequence R description Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX source Swiss-Prot : SWS_FT_FI8 35) chain D residue 76 type SITE sequence R description Self- and pathogen-derived peptide antigen => ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:23260142, ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:8145819, ECO:0007744|PDB:4FQX, ECO:0007744|PDB:4GBX source Swiss-Prot : SWS_FT_FI8 36) chain A residue 78 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400 source Swiss-Prot : SWS_FT_FI9 37) chain A residue 118 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400 source Swiss-Prot : SWS_FT_FI9 38) chain D residue 78 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400 source Swiss-Prot : SWS_FT_FI9 39) chain D residue 118 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7477400 source Swiss-Prot : SWS_FT_FI9 40) chain C residue 88-94 type prosite sequence VVHFFKN description MYELIN_MBP Myelin basic protein signature. VVHFFKN source prosite : PS00569 41) chain B residue 171-177 type prosite sequence YTCQVEH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCQVEH source prosite : PS00290 42) chain A residue 161-167 type prosite sequence YDCRVEH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCQVEH source prosite : PS00290

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