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Secondary structure of Src homology 2 domain of c-Abl by heteronouclear NMR spectroscopy in solution

Overduin, Michael and Mayer, Bruce and Rios, Carlos B. and Baltimore, David and Cowburn, David (1992) Secondary structure of Src homology 2 domain of c-Abl by heteronouclear NMR spectroscopy in solution. Proceedings of the National Academy of Sciences of the United States of America, 89 (24). pp. 11673-11677. ISSN 0027-8424. PMCID PMC50618. doi:10.1073/pnas.89.24.11673.

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The Src homology 2 (SH2) domain is a recognition motif thought to mediate the association of the cytoplasmic proteins involved in signal transduction by binding to phosphotyrosyl-containing sequences in proteins. Assignments of nearly all 1H and 15N resonances of the SH2 domain from the c-Abl protein-tyrosine kinase have been obtained from homonuclear and heteronuclear NMR experiments. The secondary structure has been elucidated from the pattern of nuclear Overhauser effects, from vicinal coupling constants, and from observation of slowly exchanging amino hydrogens. The secondary structure contains two α-helices and eight β-strands, six of which are arranged in two contiguous, antiparallel β-sheets. Residues believed to be involved in phosphotyrosyl ligand binding are on a face of one β-sheet. The alignment of homologous sequences on the basis of secondary structure suggests a conserved global fold in a family of SH2 domains.

Item Type:Article
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URLURL TypeDescription CentralArticle
Baltimore, David0000-0001-8723-8190
Additional Information:© 1992 by the National Academy of Sciences. Contributed by David Baltimore, July 14, 1992. We are grateful to Prof. John Kuriyan, Dr. Nalin Pant, and Dr. Yuying Gosser for discussion. This work was supported by grants (D.B., CA51462; D.C., DK20357 and GM47021) and fellowships (B.M., CA0887501; C.B.R., GM14313) from the National Institutes of Health. NMR resources were purchased with grants from the National Institutes of Health, the Keck Foundation, and the National Science Foundation. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funding AgencyGrant Number
NIH Predoctoral FellowshipCA0887501
NIH Predoctoral FellowshipGM14313
W. M. Keck FoundationUNSPECIFIED
Subject Keywords:oncogene; c-abl
Issue or Number:24
PubMed Central ID:PMC50618
Record Number:CaltechAUTHORS:OVEpnas92
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Official Citation:Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution M Overduin, B Mayer, C B Rios, D Baltimore, D Cowburn Proceedings of the National Academy of Sciences Dec 1992, 89 (24) 11673-11677; DOI: 10.1073/pnas.89.24.11673
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:7747
Deposited By: Tony Diaz
Deposited On:01 Aug 2007
Last Modified:08 Nov 2021 20:45

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