2h7d | pdb_00002h7d

Solution structure of the talin F3 domain in complex with a chimeric beta3 integrin-PIP kinase peptide

spinqualitylabelsall models 2h7d Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h7d is a 2 chain structure with sequence from Gallus gallus and Mus musculus. The February 2011 RCSB PDB Molecule of the Month feature on Integrin by David Goodsell is 10.2210/rcsb_pdb/mom_2011_2. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: PTR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TLN1_CHICK Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a high molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Regulation of integrin affinity (activation) is essential for metazoan development and for many pathological processes. Binding of the talin phosphotyrosine-binding (PTB) domain to integrin beta subunit cytoplasmic domains (tails) causes activation, whereas numerous other PTB-domain-containing proteins bind integrins without activating them. Here we define the structure of a complex between talin and the membrane-proximal integrin beta3 cytoplasmic domain and identify specific contacts between talin and the integrin tail required for activation. We used structure-based mutagenesis to engineer talin and beta3 variants that interact with comparable affinity to the wild-type proteins but inhibit integrin activation by competing with endogenous talin. These results reveal the structural basis of talin's unique ability to activate integrins, identify an interaction that could aid in the design of therapeutics to block integrin activation, and enable engineering of cells with defects in the activation of multiple classes of integrins. Structural basis of integrin activation by talin.,Wegener KL, Partridge AW, Han J, Pickford AR, Liddington RC, Ginsberg MH, Campbell ID Cell. 2007 Jan 12;128(1):171-82. PMID:17218263 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Talin 3D structures

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