1H and 15N assignments and secondary structure of the Src SH3 domain.

FEBS Lett

Authors	Yu M Rosen S Schreiber
Keywords	Protein-Tyrosine Kinases Molecular Sequence Data Amino Acid Sequence Models, Molecular Recombinant Fusion Proteins Escherichia coli Cloning, Molecular Sequence Homology, Amino Acid Hydrogen Protein Structure, Secondary Protein Folding Magnetic Resonance Spectroscopy Glutathione Transferase Genes, src Nitrogen Isotopes
Abstract	The 1H and 15N sequential assignments of the Src SH3 domain have been determined through a combination of 2D and 3D Nuclear Magnetic Resonance (NMR) methods. The secondary structure of the protein has been identified based on long-range NOE patterns. The SH3 domain of Src consists largely of six beta-strands that form two anti-parallel beta-sheets.
Year of Publication	1993
Journal	FEBS Lett
Volume	324
Issue	1
Pages	87-92
Date Published	1993 Jun 07
ISSN	0014-5793
PubMed ID	8504863
Links	PubMed Google Scholar
Grant list	GM44993 / GM / NIGMS NIH HHS / United States

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