7Z50: PDB entry 7Z50
Structure of the highly diabetogenic 4.1-T cell receptor targeting a hybrid insulin peptide bound to I-Ag7. Determined by X-ray diffraction at 2.65 Å resolution. Released 20 Jul 2022.
- Method
- X-ray diffraction
- Resolution
- 2.65 Å
- Organism
- Mus musculus
- Chains
- 10
- Atoms
- 12,716
- Mol. weight
- 204.27 kDa
- Ligands
- NAG
- Released
- 20 Jul 2022
Explore 7Z50 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7Z50 contains 48 α-helices and 141 β-strands across 10 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 3 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-17 | 12 | 1 |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 42-45 | 4 | 1 |
| α-helix | 48-53 | 6 | |
| β-strand | 55 | 1 | 2 |
| α-helix | 59-78 | 20 | |
| α-helix | 82-87 | 6 | |
| β-strand | 90-95 | 6 | 3 |
| β-strand | 105-114 | 10 | 3 |
| β-strand | 120-125 | 6 | 4 |
| β-strand | 128-130 | 3 | 4 |
| β-strand | 134-136 | 3 | 3 |
| β-strand | 140-141 | 2 | 3 |
| β-strand | 147-155 | 9 | 3 |
| β-strand | 163-168 | 6 | 4 |
| β-strand | 176-180 | 5 | 4 |
Chain B: 8 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 46-49 | 4 | 1 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-64 | 10 | |
| α-helix | 66-72 | 7 | |
| α-helix | 73-78 | 6 | |
| α-helix | 79-80 | 2 | |
| α-helix | 81-85 | 5 | |
| α-helix | 86-88 | 3 | |
| β-strand | 94 | 1 | 5 |
| β-strand | 97-102 | 6 | 6 |
| β-strand | 113-121 | 9 | 6 |
| β-strand | 122 | 1 | 5 |
| β-strand | 127-132 | 6 | 7 |
| β-strand | 135-137 | 3 | 7 |
| β-strand | 141-143 | 3 | 6 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-148 | 2 | 6 |
| β-strand | 154-161 | 8 | 6 |
| β-strand | 170-175 | 6 | 7 |
| β-strand | 183-187 | 5 | 7 |
Chain C: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-9 | 4 | 8 |
| β-strand | 13-17 | 5 | 8 |
| β-strand | 21-28 | 8 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 42-45 | 4 | 8 |
| α-helix | 48-53 | 6 | |
| β-strand | 55 | 1 | 9 |
| α-helix | 59-78 | 20 | |
| α-helix | 83-87 | 5 | |
| β-strand | 90-95 | 6 | 10 |
| β-strand | 105-114 | 10 | 10 |
| β-strand | 120-125 | 6 | 11 |
| β-strand | 128-129 | 2 | 11 |
| β-strand | 134-136 | 3 | 10 |
| β-strand | 140-141 | 2 | 10 |
| β-strand | 147-155 | 9 | 10 |
| β-strand | 163-168 | 6 | 11 |
| β-strand | 176-180 | 5 | 11 |
Chain D: 8 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 8 |
| β-strand | 23-32 | 10 | 8 |
| β-strand | 35-41 | 7 | 8 |
| β-strand | 46-49 | 4 | 8 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-64 | 10 | |
| α-helix | 66-72 | 7 | |
| α-helix | 73-78 | 6 | |
| α-helix | 79-80 | 2 | |
| α-helix | 81-85 | 5 | |
| α-helix | 86-88 | 3 | |
| β-strand | 94 | 1 | 12 |
| β-strand | 97-102 | 6 | 13 |
| β-strand | 113-121 | 9 | 13 |
| β-strand | 122 | 1 | 12 |
| β-strand | 127-132 | 6 | 14 |
| β-strand | 135-137 | 3 | 14 |
| β-strand | 141-143 | 3 | 13 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-148 | 2 | 13 |
| β-strand | 154-161 | 8 | 13 |
| β-strand | 170-175 | 6 | 14 |
| β-strand | 183-186 | 4 | 14 |
Chain E: 8 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-6 | 3 | 15 |
| β-strand | 9-13 | 5 | 16 |
| β-strand | 18-23 | 6 | 15 |
| α-helix | 24-25 | 2 | |
| β-strand | 30-37 | 8 | 16 |
| β-strand | 41-49 | 9 | 16 |
| β-strand | 52-55 | 4 | 16 |
| β-strand | 64-67 | 4 | 15 |
| β-strand | 74-78 | 5 | 15 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-94 | 8 | 16 |
| β-strand | 102-103 | 2 | 16 |
| β-strand | 107-112 | 6 | 16 |
| α-helix | 115-117 | 3 | |
| β-strand | 119 | 1 | 17 |
| α-helix | 120-121 | 2 | |
| β-strand | 122-126 | 5 | 18 |
| α-helix | 127-129 | 3 | |
| α-helix | 130-136 | 7 | |
| β-strand | 138-148 | 11 | 18 |
| β-strand | 149 | 1 | 17 |
| β-strand | 153-159 | 7 | 19 |
| β-strand | 162-164 | 3 | 19 |
| β-strand | 168-170 | 3 | 18 |
| β-strand | 175-176 | 2 | 18 |
| β-strand | 186-195 | 10 | 18 |
| α-helix | 196-200 | 5 | |
| β-strand | 205-212 | 8 | 19 |
| β-strand | 215 | 1 | 20 |
| α-helix | 226-227 | 2 | |
| β-strand | 229 | 1 | 20 |
| β-strand | 231-238 | 8 | 19 |
Chain F: 10 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-6 | 3 | 21 |
| β-strand | 9-13 | 5 | 22 |
| β-strand | 18-23 | 6 | 21 |
| α-helix | 24-25 | 2 | |
| β-strand | 30-37 | 8 | 22 |
| β-strand | 41-49 | 9 | 22 |
| β-strand | 52-55 | 4 | 22 |
| α-helix | 60 | 1 | |
| β-strand | 64-67 | 4 | 21 |
| β-strand | 74-78 | 5 | 21 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-94 | 8 | 22 |
| β-strand | 102-103 | 2 | 22 |
| β-strand | 107-112 | 6 | 22 |
| α-helix | 115-117 | 3 | |
| β-strand | 119 | 1 | 23 |
| α-helix | 120-121 | 2 | |
| β-strand | 122-126 | 5 | 24 |
| α-helix | 127-129 | 3 | |
| α-helix | 130-136 | 7 | |
| β-strand | 138-148 | 11 | 24 |
| β-strand | 149 | 1 | 23 |
| β-strand | 153-159 | 7 | 25 |
| β-strand | 162-164 | 3 | 25 |
| β-strand | 168-170 | 3 | 24 |
| α-helix | 174 | 1 | |
| β-strand | 175-176 | 2 | 24 |
| β-strand | 186-195 | 10 | 24 |
| α-helix | 196-200 | 5 | |
| β-strand | 205-212 | 8 | 25 |
| β-strand | 215 | 1 | 26 |
| α-helix | 226-227 | 2 | |
| β-strand | 229 | 1 | 26 |
| β-strand | 231-238 | 8 | 25 |
Chain G: 3 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 27 |
| β-strand | 11-15 | 5 | 28 |
| β-strand | 20-26 | 7 | 27 |
| β-strand | 33-39 | 7 | 28 |
| β-strand | 46-52 | 7 | 28 |
| β-strand | 57-59 | 3 | 27 |
| β-strand | 63-68 | 6 | 27 |
| β-strand | 73-78 | 6 | 27 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-94 | 8 | 28 |
| β-strand | 100-102 | 3 | 28 |
| β-strand | 106-111 | 6 | 28 |
| β-strand | 120-124 | 5 | 29 |
| α-helix | 125-126 | 2 | |
| β-strand | 133-138 | 6 | 29 |
| β-strand | 154-156 | 3 | 29 |
| α-helix | 157-159 | 3 | |
| β-strand | 160-164 | 5 | 29 |
| β-strand | 169-178 | 10 | 29 |
Chain H: 3 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 30 |
| β-strand | 11-15 | 5 | 31 |
| β-strand | 20-26 | 7 | 30 |
| β-strand | 33-39 | 7 | 31 |
| β-strand | 46-52 | 7 | 31 |
| β-strand | 57-59 | 3 | 30 |
| β-strand | 63-68 | 6 | 30 |
| β-strand | 73-78 | 6 | 30 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-94 | 8 | 31 |
| β-strand | 100-102 | 3 | 31 |
| β-strand | 106-111 | 6 | 31 |
| β-strand | 120-124 | 5 | 32 |
| α-helix | 125-127 | 3 | |
| β-strand | 133-140 | 8 | 32 |
| β-strand | 154-156 | 3 | 32 |
| α-helix | 157-159 | 3 | |
| β-strand | 160-163 | 4 | 32 |
| β-strand | 170-178 | 9 | 32 |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| H-2 class II histocompatibility antigen, A-D alpha chain | A, C | protein | 202 | Mus musculus | P04228 (AlphaFold model) |
| H2-Ab1 protein | B, D | protein | 230 | Mus musculus | Q31135 (AlphaFold model) |
| 4.1 TCR beta chain | E, F | protein | 242 | Mus musculus | |
| 4.1 TCR alpha chain | G, H | protein | 207 | Mus musculus | |
| Hybrid insulin peptide | T, W | protein | 15 | Mus musculus | |
Sequence of entity 1 (A, C), FASTA
>7Z50_1 H-2 class II histocompatibility antigen, A-D alpha chain (chains A, C)
EDDIEADHVGFYGTTVYQSPGDIGQYTHEFDGDELFYVDLDKKKTVWRLPEFGQLILFEP
QGGLQNIAAEKHNLGCLTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPV
INITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLK
HWEPEIPAPMSELTESLEVLFQ
Sequence of entity 2 (B, D), FASTA
>7Z50_2 H2-Ab1 protein (chains B, D)
LQTLALEVEDDPCGGGGGSGGGSGGSGDSERHFVHQFKGECYFTNGTQRIRLVTRYIYNR
EEYLRFDSDVGEYRAVTELGRHSAEYYNKQYLERTRAELDTACRHNYEETEVPTSLRRLE
QPNVAISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTF
QVLVMLEMTPHQGEVYTCHVEHPSLKSPITVEWRAQSESARSKSLEVLFQ
Sequence of entity 3 (E, F), FASTA
>7Z50_3 4.1 TCR beta chain (chains E, F)
MGVIQTPRHKVTGKGQEATLWCEPISGHSAVFWYRQTIVQGLEFLTYFRNQAPIDDSGMP
KERFSAQMPNQSHSTLKIQSTQPQDSAVYLCASSRQGQNTLYFGAGTRLSVLEDLKNVFP
PEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPA
LNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
Sequence of entity 4 (G, H), FASTA
>7Z50_4 4.1 TCR alpha chain (chains G, H)
MGEQVEQLPSILRVQEGSSASINCSYEDSASNYFPWYKQEPGENPKLIIDIRSNMERKQT
QGLIVLLDKKAKRFSLHITDTQPGDSAMYFCAASVRNYKYVFGAGTRLKVIADIQNPDPA
VYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNK
SDFACANAFNNSIIPEDTFFPSPESSA
Sequence of entity 5 (T, W), FASTA
>7Z50_5 Hybrid insulin peptide (chains T, W)
LQTLALEVEDDPCGG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
Water and common crystallization additives (CL, NA, EDO) are not listed.
Primary citation
Structural plasticity in I-A g7 links autoreactivity to hybrid insulin peptides in type I diabetes. Erausquin, E., Serra, P., Parras, D. et al. Front Immunol (2022) 13:924311-924311. DOI 10.3389/fimmu.2022.924311 · PubMed
Other PDB entries of the same protein (UniProt P04228 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6BLQ 1.8 Å, Crystal Structure of IAg7 in complex with insulin mimotope p8E9E
- 7QHP 1.82 Å, Structure of I-Ag7 with a bound hybrid insulin peptide
- 6BLR 1.96 Å, Crystal Structure of IAg7 in complex with insulin mimotope p8E9E6SS
- 6BLX 2.32 Å, Crystal structure of IAg7 in complex with insulin mimotope p8G9E
- 2IAD 2.4 Å, Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138
- 5DMK 2.45 Å, Crystal Structure of IAg7 in complex with RLGL-WE14
- 1ES0 2.6 Å, Crystal structure of the murine class II allele I-A(G7) complexed with the glutamic acid…
- 1IAO 2.6 Å, Class II MHC I-ad in complex with ovalbumin peptide 323-339
- 3MBE 2.89 Å, TCR 21.30 in complex with MHC class II I-Ag7HEL(11-27)
- 7RDV 2.9 Å, TFH TCR bound to MHC Class II IAd presenting aggrecan epitope
- 3CUP 3.09 Å, Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide…
- 1F3J 3.1 Å, Histocompatibility antigen I-AG7
Browse structure collections
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