4um9 | pdb_00004um9

Crystal structure of alpha V beta 6 with peptide

spinqualitylabelsall models 4um9, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4um9 is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, CA, MAN, MG, NAG, SO4 NonStd Res: ACE, NHH Related: 4um8 Resources: FirstGlance, OCA, RCSB, PDBsum Disease [ITB6_HUMAN] Hypocalcified amelogenesis imperfecta;Hypoplastic amelogenesis imperfecta. Function [ITAV_HUMAN] The alpha-V 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. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. [ITB6_HUMAN] Integrin alpha-V/beta-6 is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion. Publication Abstract from PubMed Eight integrin alpha-beta 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 alphaVbeta6 binds with high affinity to a RGDLXXL/I motif within the prodomains of TGF-beta1 and TGF-beta3. The LXXL/I motif forms an amphipathic alpha-helix that binds in a hydrophobic pocket in the beta6 subunit. Elucidation of the basis for ligand binding specificity by the integrin beta subunit reveals contributions by three different betaI-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 beta subunit in integrin evolution, thus suggesting a paradigmatic role in overall beta-subunit function. Structural determinants of integrin beta-subunit specificity for latent TGF-beta,Dong X, Hudson NE, Lu C, Springer TA Nat Struct Mol Biol. 2014 Nov 10. doi: 10.1038/nsmb.2905. PMID:25383667 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA