The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

STRUCTURAL BASIS OF SH2 DOMAIN MUTATIONS IN X-LINKED AGAMMAGLOBULINEMIA

Author

Summary, in English

The three-dimensional structure of Bruton's agammaloglobulinemia tyrosine kinase (Btk) SH2 domain was modeled based on v-Src. Btk SH2 is presumably very related to the other SH2 structures consisting of two beta-sheets surrounded by two alpha-helices, with a well conserved hydrophobic core and phoshotyrosyl peptide binding site. The model was used to predict the recognition sequence of the target protein, which probably is YEXI/L. Mutations in the Btk sequence can cause the human disease X-linked agammaglobulinemia and reasons for the disease in Btk SH2 mutations were inferred from the model. (C) 1994 Academic Press, Inc.

Publishing year

1994

Language

English

Pages

1270-1277

Publication/Series

Biochemical and Biophysical Research Communications

Volume

205

Issue

2

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Status

Published

ISBN/ISSN/Other

  • ISSN: 1090-2104