3sem

SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR

spinqualitylabelsall models 3sem, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sem is a 4 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: NMC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SEM5_CAEEL Acts both in vulval induction and sex myoblast migration. Presumably interacts with the kinase receptor let-23 and with a target that modifies the Ras-like protein let-60. 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.

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