1shf
CRYSTAL STRUCTURE OF THE SH3 DOMAIN IN HUMAN FYN; COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SH3 DOMAINS IN TYROSINE KINASES AND SPECTRIN
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OverviewOverview
The Src-homology 3 (SH3) region is a protein domain consisting of, approximately 60 residues. It occurs in a large number of eukaryotic, proteins involved in signal transduction, cell polarization and, membrane--cytoskeleton interactions. The function is unknown, but it is, probably involved in specific protein--protein interactions. Here we, report the crystal structure of the SH3 domain of Fyn (a Src family, tyrosine kinase) at 1.9 A resolution. The crystals have two SH3 molecules, per asymmetric unit. These two Fyn SH3 domains are not related by a local, twofold axis. The crystal structures of spectrin and Fyn SH3 domains as, well as the solution structure of the Src SH3 domain show that these all, have the same basic fold. A protein domain which has the same topology as, SH3 is present in the prokaryotic regulatory enzyme BirA. The comparison, between the crystal structures of Fyn and spectrin SH3 domains shows that, a conserved surface patch, consisting mainly of aromatic residues, is, flanked by two hairpin-like loops (residues 94-104 and 114-118 in Fyn)., These loops are different in tyrosine kinase and spectrin SH3 domains., They could modulate the binding properties of the aromatic surface.
About this StructureAbout this Structure
1SHF is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin., Noble ME, Musacchio A, Saraste M, Courtneidge SA, Wierenga RK, EMBO J. 1993 Jul;12(7):2617-24. PMID:7687536
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