4UM9
Crystal structure of alpha V beta 6 with peptide
Summary for 4UM9
| Entry DOI | 10.2210/pdb4um9/pdb |
| Related | 4UM8 |
| Descriptor | Integrin alpha-V heavy chain, CALCIUM ION, MAGNESIUM ION, ... (14 entities in total) |
| Functional Keywords | immune system, cell surface receptor |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 250392.60 |
| Authors | Dong, X.,Springer, T.A. (deposition date: 2014-05-15, release date: 2014-11-12, Last modification date: 2024-11-06) |
| Primary citation | Dong, X.,Hudson, N.E.,Lu, C.,Springer, T.A. Structural Determinants of Integrin Beta-Subunit Specificity for Latent Tgf-Beta Nat.Struct.Mol.Biol., 21:1091-, 2014 Cited by PubMed Abstract: Eight integrin α-β heterodimers recognize ligands with an Arg-Gly-Asp (RGD) motif. However, the structural mechanism by which integrins differentiate among extracellular proteins with RGD motifs is not understood. Here, crystal structures, mutations and peptide-affinity measurements show that αVβ6 binds with high affinity to a RGDLXXL/I motif within the prodomains of TGF-β1 and TGF-β3. The LXXL/I motif forms an amphipathic α-helix that binds in a hydrophobic pocket in the β6 subunit. Elucidation of the basis for ligand binding specificity by the integrin β subunit reveals contributions by three different βI-domain loops, which we designate specificity-determining loops (SDLs) 1, 2 and 3. Variation in a pair of single key residues in SDL1 and SDL3 correlates with the variation of the entire β subunit in integrin evolution, thus suggesting a paradigmatic role in overall β-subunit function. PubMed: 25383667DOI: 10.1038/NSMB.2905 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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