1b07

CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR

spinqualitylabelsall models 1b07, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b07 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PYJ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CRK_MOUSE] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. 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 Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich sequences. However, instead of recognizing critical prolines on the basis of side chain shape or rigidity, these domains broadly accepted amide N-substituted residues. Proline is apparently specifically selected in vivo, despite low complementarity, because it is the only endogenous N-substituted amino acid. This discriminatory mechanism explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The mechanism can be exploited: screening a series of ligands in which key prolines were replaced by nonnatural N-substituted residues yielded a ligand that selectively bound the Grb2 SH3 domain with 100 times greater affinity. Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors.,Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA Science. 1998 Dec 11;282(5396):2088-92. PMID:9851931 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adapter molecule crk 3D structures Non-Standard Residue

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