8VDU: Hybrid insulin peptide
Crystal structure of hybrid insulin peptide (InsC8-15-IAPP74-80) bound to HLA-DQ8. Determined by X-ray diffraction at 3.5 Å resolution. Released 7 Aug 2024.
- Method
- X-ray diffraction
- Resolution
- 3.5 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 12,192
- Mol. weight
- 182.22 kDa
- Ligands
- NAG
- Released
- 7 Aug 2024
Explore 8VDU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8VDU contains 43 α-helices and 120 β-strands across 12 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: 4 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-14 | 11 | 1 |
| β-strand | 20-26 | 7 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 46-51 | 6 | |
| β-strand | 54 | 1 | 2 |
| α-helix | 57-76 | 20 | |
| α-helix | 81-87 | 7 | |
| β-strand | 88-93 | 6 | 3 |
| β-strand | 103-112 | 10 | 3 |
| β-strand | 117-123 | 7 | 4 |
| β-strand | 126-127 | 2 | 4 |
| α-helix | 128 | 1 | |
| β-strand | 132-134 | 3 | 3 |
| β-strand | 138-139 | 2 | 3 |
| β-strand | 145-153 | 9 | 3 |
| β-strand | 161-167 | 7 | 4 |
| β-strand | 174-178 | 5 | 4 |
Chain B: 7 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-18 | 11 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 55-63 | 9 | |
| α-helix | 65-72 | 8 | |
| α-helix | 74 | 1 | |
| α-helix | 75-79 | 5 | |
| α-helix | 80-86 | 7 | |
| α-helix | 90-92 | 3 | |
| β-strand | 95 | 1 | 5 |
| β-strand | 98-103 | 6 | 6 |
| β-strand | 115-122 | 8 | 6 |
| β-strand | 123 | 1 | 5 |
| β-strand | 128-133 | 6 | 7 |
| β-strand | 136-137 | 2 | 7 |
| β-strand | 142-144 | 3 | 6 |
| α-helix | 145-147 | 3 | |
| β-strand | 148-149 | 2 | 6 |
| β-strand | 155-161 | 7 | 6 |
| β-strand | 170-176 | 7 | 7 |
| β-strand | 184-189 | 6 | 7 |
Chain C: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 2 |
| α-helix | 6-11 | 6 | |
Chain D: 4 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-14 | 11 | 8 |
| β-strand | 19-26 | 8 | 8 |
| β-strand | 29-35 | 7 | 8 |
| β-strand | 40-43 | 4 | 8 |
| α-helix | 46-51 | 6 | |
| β-strand | 53 | 1 | 9 |
| α-helix | 57-76 | 20 | |
| α-helix | 81-87 | 7 | |
| β-strand | 88-93 | 6 | 10 |
| β-strand | 103-112 | 10 | 10 |
| β-strand | 118-123 | 6 | 11 |
| β-strand | 126-127 | 2 | 11 |
| α-helix | 128 | 1 | |
| β-strand | 132-134 | 3 | 10 |
| β-strand | 138-139 | 2 | 10 |
| β-strand | 145-153 | 9 | 10 |
| β-strand | 161-166 | 6 | 11 |
| β-strand | 174-178 | 5 | 11 |
Chain E: 6 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-18 | 11 | 8 |
| β-strand | 23-32 | 10 | 8 |
| β-strand | 35-41 | 7 | 8 |
| β-strand | 47-49 | 3 | 8 |
| α-helix | 55-63 | 9 | |
| α-helix | 65-72 | 8 | |
| α-helix | 74 | 1 | |
| α-helix | 75-79 | 5 | |
| α-helix | 80-86 | 7 | |
| β-strand | 95 | 1 | 12 |
| β-strand | 99-103 | 5 | 13 |
| β-strand | 113-122 | 10 | 13 |
| β-strand | 123 | 1 | 12 |
| β-strand | 128-133 | 6 | 14 |
| β-strand | 136-137 | 2 | 14 |
| β-strand | 142-144 | 3 | 13 |
| α-helix | 145-147 | 3 | |
| β-strand | 148-149 | 2 | 13 |
| β-strand | 155-163 | 9 | 13 |
| β-strand | 170-176 | 7 | 14 |
| β-strand | 184-189 | 6 | 14 |
Chain F: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 9 |
| α-helix | 7-12 | 6 | |
Chain G: 3 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-14 | 11 | 15 |
| β-strand | 20-26 | 7 | 15 |
| β-strand | 29-35 | 7 | 15 |
| β-strand | 40-43 | 4 | 15 |
| α-helix | 46-51 | 6 | |
| β-strand | 53-54 | 2 | 16 |
| α-helix | 57-76 | 20 | |
| α-helix | 81-87 | 7 | |
| β-strand | 88-93 | 6 | 17 |
| β-strand | 103-112 | 10 | 17 |
| β-strand | 118-123 | 6 | 18 |
| β-strand | 126-128 | 3 | 18 |
| β-strand | 132-134 | 3 | 17 |
| β-strand | 138-139 | 2 | 17 |
| β-strand | 145-153 | 9 | 17 |
| β-strand | 161-166 | 6 | 18 |
| β-strand | 174-178 | 5 | 18 |
Chains H and K: 6 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-18 | 11 | 15 |
| β-strand | 23-32 | 10 | 15 |
| β-strand | 35-41 | 7 | 15 |
| β-strand | 47-49 | 3 | 15 |
| α-helix | 55-63 | 9 | |
| α-helix | 65-72 | 8 | |
| α-helix | 74 | 1 | |
| α-helix | 75-79 | 5 | |
| α-helix | 80-86 | 7 | |
| β-strand | 95 | 1 | 19 |
| β-strand | 98-103 | 6 | 20 |
| β-strand | 113-122 | 10 | 20 |
| β-strand | 123 | 1 | 19 |
| β-strand | 128-133 | 6 | 21 |
| β-strand | 136-137 | 2 | 21 |
| β-strand | 142-144 | 3 | 20 |
| α-helix | 145-147 | 3 | |
| β-strand | 148-149 | 2 | 20 |
| β-strand | 155-163 | 9 | 20 |
| β-strand | 170-176 | 7 | 21 |
| β-strand | 184-189 | 6 | 21 |
3 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 |
|---|
| MHC class II HLA-DQ-alpha chain | A, D, G, J | protein | 185 | Homo sapiens | Q30069 (AlphaFold model) |
| MHC class II HLA-DQ-beta-1 | B, E, H, K | protein | 192 | Homo sapiens | O19707 (AlphaFold model) |
| Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80) | C, F, I, L | protein | 15 | Homo sapiens | |
Sequence of entity 1 (A, D, G, J), FASTA
>8VDU_1 MHC class II HLA-DQ-alpha chain (chains A, D, G, J)
EDIVADHVASYGVNLYQSYGPSGQYSHEFDGDEEFYVDLERKETVWQLPLFRRFRRFDPQ
FALTNIAVLKHNLNCVIKRSNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVDNIFPPVV
NITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDEPLLKH
WEPES
Sequence of entity 2 (B, E, H, K), FASTA
>8VDU_2 MHC class II HLA-DQ-beta-1 (chains B, E, H, K)
RDSPEDFVYQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVGVYRAVTPLGPPAAEY
WNSQKEVLERTRAELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVT
DFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTFQILVMLEMTPQRGDVYTCHVEHPSL
QNPIIVEWRAQS
Sequence of entity 3 (C, F, I, L), FASTA
>8VDU_3 Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80) (chains C, F, I, L)
GQVELGGGNAVEVCK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (PEG) are not listed.
Primary citation
A structural basis of T cell cross-reactivity to native and spliced self-antigens presented by HLA-DQ8. Tran, M.T., Lim, J.J., Loh, T.J. et al. J Biol Chem (2024) 300:107612-107612. DOI 10.1016/j.jbc.2024.107612 · PubMed
Other PDB entries of the same protein (UniProt Q30069 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6DFX 2.03 Å, human diabetogenic TCR T1D3 in complex with DQ8-p8E9E peptide
- 6XC9 2.4 Å, Immune receptor complex
- 8VD0 2.4 Å, Human TCR ET650-4 in complex with DQ8-InsC8-15-IAPP2
- 5KS9 2.55 Å, Bel502-DQ8-glia-alpha1 complex
- 8VCX 2.59 Å, Human TCR A2.13 in complex with DQ8-InsCpep
- 8VCY 2.6 Å, Human TCR A2.13 in complex with DQ8-InsC8-15NPY
- 8VDD 2.6 Å, Crystal structure of Proinsulin C-peptide bound to HLA-DQ8
- 4Z7V 2.65 Å, L3-12 complex
- 4Z7U 2.7 Å, S13 complex
- 4Z7W 2.89 Å, T316 complex
- 6XCO 2.9 Å, Immune receptor complex
- 8VD2 2.9 Å, Human TCR ET650-4 in complex with DQ8-InsC8-15-IAPP1
Browse structure collections
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