1nlo | pdb_00001nlo

STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE

spinqualitylabelsall models 1nlo, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nlo is a 2 chain structure with sequence from Chick. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ACE, MN1, MN2, MN7, NH2 Gene: CHICKEN (CHICK) Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [SRC_AVISR] This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. 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 BACKGROUND: Protein-structure-based combinatorial chemistry has recently been used to discover several ligands containing non-peptide binding elements to the Src SH3 domain. The encoded library used has the form Cap-M1-M2-M3-PLPPLP, in which the Cap and Mi's are composed of a diverse set of organic monomers. The PLPPLP portion provided a structural bias directing the non-peptide fragment Cap-M1-M2-M3 to the SH3 specificity pocket. Fifteen ligands were selected from > 1.1 million distinct compounds. The structural basis for selection was unknown. RESULTS: The solution structures of the Src SH3 domain complexed with two ligands containing non-peptide elements selected from the library were determined by multidimensional NMR spectroscopy. The non-peptide moieties of the ligands interact with the specificity pocket of Src SH3 domain differently from peptides complexed with SH3 domains. Structural information about the ligands was used to design various homologs, whose affinities for the SH3 domain were measured. The results provide a structural basis for understanding the selection of a few optimal ligands from a large library. CONCLUSIONS: The cycle of protein-structure-based combinatorial chemistry followed by structure determination of the few highest affinity ligands provides a powerful new tool for the field of molecular recognition. Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesis.,Feng S, Kapoor TM, Shirai F, Combs AP, Schreiber SL Chem Biol. 1996 Aug;3(8):661-70. PMID:8807900 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoclonal Antibody Tyrosine kinase

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