Integrin alpha-V (ITGAV) is a 1048-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06756.
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The mean pLDDT of this model is 88.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 73% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677).…
Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3), beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8). Interacts with CIB1 (PubMed:24011356). Interacts with RAB25 (PubMed:17925226). Integrins ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via…
Cell membrane, Cell junction, focal adhesion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9CZD | X-ray | 2.23 Å | A=31-625 |
| 5FFG | X-ray | 2.25 Å | A=31-627 |
| 8W30 | X-ray | 2.45 Å | A=31-625 |
| 9CZA | X-ray | 2.49 Å | A=31-625 |
| 4UM9 | X-ray | 2.5 Å | A/C=31-625 |
| 9CZF | X-ray | 2.53 Å | A=31-625 |
| 9CZ7 | X-ray | 2.57 Å | A=31-625 |
| 6OM1 | X-ray | 2.66 Å | A/C/E/G=31-624 |
| 8VS6 | EM | 2.73 Å | A=31-992 |
| 6OM2 | X-ray | 2.77 Å | A/C=31-624 |
| 9IUJ | EM | 2.78 Å | A=31-987 |
| 8XEL | EM | 2.8 Å | A=1-1048 |
| 8XFG | EM | 2.8 Å | A=1-1048 |
| 4UM8 | X-ray | 2.85 Å | A/C=31-625 |
| 9IND | EM | 2.88 Å | A=31-470 |
| 9XMM | EM | 2.88 Å | A=31-624 |
| 3IJE | X-ray | 2.9 Å | A=31-997 |
| 4G1M | X-ray | 2.9 Å | A=31-989 |
| 8TCF | EM | 2.9 Å | A=31-473 |
| 8XEI | EM | 2.9 Å | A=1-1048 |
Showing 20 of 58 experimental structures (best resolution first).
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