spacer SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA
Primary citation
Title Solution structure of the SH3 domain of phospholipase C-gamma.
Authors Kohda, D.search; Hatanaka, H.search; Odaka, M.search; Mandiyan, V.search; Ullrich, A.search; Schlessinger, J.search; Inagaki, F.search
Journal CELL(CAMBRIDGE,MASS.)search vol:72, pag:953-960 (1993), Identifiers: PubMed ID (7681365)search DOI (10.1016/0092-8674(93)90583-C)
Abstract SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-gamma (PLC-gamma) was determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of eight antiparallel beta strands consisting of two successive "Greek key" motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of beta structure, the SH3 domain of PLC-gamma is flexible.
MeSH terms Amino Acid Sequencesearch, Binding Sitessearch, Humanssearch, Hydrogen Bondingsearch, Magnetic Resonance Spectroscopysearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Motionsearch, Protein Structuresearch, Secondarysearch, Protein Structuresearch, Tertiarysearch, Proto-Oncogene Proteins pp60(c-src)search, Recombinant Fusion Proteinssearch, Spectrinsearch, Type C Phospholipasessearch
Other entries described in this publication 2hsp
Secondary citations
Title Solution Structure and Ligand-Binding Site of the C-Terminal SH3 Domain of Grb2
Authors Kohda, D.search; Terasawa, H.search; Ichikawa, S.search; Ogura, K.search; Hatanaka, H.search; Mandiyan, V.search; Ullrich, A.search; Schlessinger, J.search; Inagaki, F.search
Journal STRUCTUREsearch vol:2, pag:1029-1040 (1994)
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