Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR. Determined by X-ray diffraction at 1.92 Å resolution. Released 3 Apr 2007.
Explore 2IAL in 3D Show helices and sheets RCSB PDB PDBe
2IAL contains 23 α-helices and 88 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 1 |
| β-strand | 9-13 | 5 | 2 |
| β-strand | 18-24 | 7 | 1 |
| β-strand | 28-36 | 9 | 2 |
| β-strand | 42-47 | 6 | 2 |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 58-63 | 6 | 1 |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 82-90 | 9 | 2 |
| β-strand | 95-98 | 4 | 2 |
| β-strand | 102-107 | 6 | 2 |
| β-strand | 116-121 | 6 | 3 |
| β-strand | 122 | 1 | 4 |
| β-strand | 129-134 | 6 | 3 |
| α-helix | 143-145 | 3 | |
| β-strand | 151-152 | 2 | 3 |
| α-helix | 153-155 | 3 | |
| β-strand | 156-160 | 5 | 3 |
| α-helix | 161-163 | 3 | |
| β-strand | 165-173 | 9 | 3 |
| α-helix | 181-184 | 4 | |
| β-strand | 195 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 5 |
| β-strand | 10-14 | 5 | 6 |
| β-strand | 19-21 | 3 | 7 |
| β-strand | 22-25 | 4 | 5 |
| β-strand | 31-37 | 7 | 6 |
| β-strand | 44-51 | 8 | 6 |
| β-strand | 54-57 | 4 | 6 |
| β-strand | 64-66 | 3 | 7 |
| β-strand | 73 | 1 | 5 |
| β-strand | 76-78 | 3 | 7 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-95 | 9 | 6 |
| β-strand | 98-101 | 4 | 6 |
| β-strand | 105-110 | 6 | 6 |
| α-helix | 113-115 | 3 | |
| β-strand | 117 | 1 | 8 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 4 |
| α-helix | 125-127 | 3 | |
| α-helix | 128-134 | 7 | |
| β-strand | 136-146 | 11 | 4 |
| β-strand | 147 | 1 | 8 |
| β-strand | 151-157 | 7 | 9 |
| β-strand | 160-162 | 3 | 9 |
| β-strand | 166-168 | 3 | 4 |
| β-strand | 173-174 | 2 | 4 |
| β-strand | 184-193 | 10 | 4 |
| α-helix | 194-197 | 4 | |
| β-strand | 203-210 | 8 | 9 |
| β-strand | 213 | 1 | 10 |
| β-strand | 227 | 1 | 10 |
| β-strand | 229-236 | 8 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 11 |
| β-strand | 9-13 | 5 | 12 |
| β-strand | 18-24 | 7 | 11 |
| β-strand | 28-36 | 9 | 12 |
| β-strand | 42-47 | 6 | 12 |
| β-strand | 51-55 | 5 | 11 |
| β-strand | 58-63 | 6 | 11 |
| α-helix | 64-66 | 3 | |
| β-strand | 68-73 | 6 | 11 |
| α-helix | 78-80 | 3 | |
| β-strand | 82-90 | 9 | 12 |
| β-strand | 95-98 | 4 | 12 |
| β-strand | 102-107 | 6 | 12 |
| β-strand | 116-119 | 4 | 13 |
| β-strand | 121-122 | 2 | 14 |
| β-strand | 129-134 | 6 | 13 |
| α-helix | 142-145 | 4 | |
| β-strand | 150-152 | 3 | 13 |
| α-helix | 153-155 | 3 | |
| β-strand | 156-160 | 5 | 13 |
| β-strand | 165-174 | 10 | 13 |
| α-helix | 181-184 | 4 | |
| β-strand | 195 | 1 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 15 |
| β-strand | 10-14 | 5 | 16 |
| β-strand | 19-21 | 3 | 17 |
| β-strand | 22-25 | 4 | 15 |
| β-strand | 31-37 | 7 | 16 |
| β-strand | 43-51 | 9 | 16 |
| β-strand | 54-57 | 4 | 16 |
| β-strand | 65-66 | 2 | 17 |
| β-strand | 73 | 1 | 15 |
| β-strand | 76-78 | 3 | 17 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-95 | 9 | 16 |
| β-strand | 98-101 | 4 | 16 |
| β-strand | 105-110 | 6 | 16 |
| α-helix | 113-115 | 3 | |
| β-strand | 117 | 1 | 18 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-125 | 6 | 14 |
| α-helix | 126-127 | 2 | |
| α-helix | 128-134 | 7 | |
| β-strand | 136-146 | 11 | 14 |
| β-strand | 147 | 1 | 18 |
| β-strand | 151-157 | 7 | 19 |
| β-strand | 160-162 | 3 | 19 |
| β-strand | 166-168 | 3 | 14 |
| β-strand | 173-174 | 2 | 14 |
| β-strand | 184-193 | 10 | 14 |
| α-helix | 194-197 | 4 | |
| β-strand | 203-210 | 8 | 19 |
| β-strand | 213 | 1 | 20 |
| α-helix | 224-225 | 2 | |
| β-strand | 227 | 1 | 20 |
| β-strand | 229-236 | 8 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD4+ T cell receptor E8 alpha chain | A, C | protein | 202 | Homo sapiens | P01848 (AlphaFold model) |
| CD4+ T cell receptor E8 beta chain | B, D | protein | 240 | Homo sapiens | P01850 (AlphaFold model) |
>2IAL_1 CD4+ T cell receptor E8 alpha chain (chains A, C) IQVEQSPPDLILQEGANSTLRCNFSDSVNNLQWFHQNPWGQLINLFYIPSGTKQNGRLSA TTVATERYSLLYISSSQTTDSGVYFCAALIQGAQKLVFGQGTRLTINPNIQNPDPAVYQL RDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSDFA CANAFNNSIIPEDTFFPSPESS
>2IAL_2 CD4+ T cell receptor E8 beta chain (chains B, D) NAGVTQTPKFRILKIGQSMTLQCTQDMNHNYMYWYRQDPGMGLKLIYYSVGAGITDKGEV PNGYNVSRSTTEDFPLRLELAAPSQTSVYFCASTYHGTGYFGEGSWLTVVEDLNKVFPPE VAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVNGKEVHSGVCTDPQPLKEQPALN DSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRAD
Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor. Deng, L., Langley, R.J., Brown, P.H. et al. Nat Immunol (2007) 8:398-408. DOI 10.1038/ni1447 · PubMed
Other PDB entries of the same protein (UniProt P01848 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2IAL directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.