STRUCTURAL BASIS FOR CHROMOSOME X-LINKED AGAMMAGLOBULINEMIA - A TYROSINE KINASE DISEASE

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Bibtex

@article{87a729872480472c97bc7549d81e6036,
title = "STRUCTURAL BASIS FOR CHROMOSOME X-LINKED AGAMMAGLOBULINEMIA - A TYROSINE KINASE DISEASE",
abstract = "X-linked agammaglobulinemia (XLA) is a hereditary defect of B-cell differentiation in man caused by deficiency of Bruton tyrosine kinase (BTK). A three-dimensional model for the BTK kinase domain, based on the core structure of cAMP-dependent protein kinase, was used to interpret the structural basis for disease in eight independent point mutations in patients with XLA. As Arg-525 of BTK has been thought to functionally substitute for a critical lysine residue in protein-serine kinases, the mutation Arg-525-->Gln was studied and found to abrogate the tyrosine kinase activity of BTK. All of the eight mutations (Lys-430-->Glu, Arg-520-->Glu, Arg-525-->Gln, Arg-562-->Pro, Ala-582-->Val, Glu-589-->Gly, Gly-594-->Glu, and Gly-613-->Asp) were located on one face of the BTK kinase domain, indicating structural clustering of functionally important residues.",
keywords = "BRUTON TYROSINE KINASE, BTK, CYTOPLASMIC TYROSINE KINASE, SIGNAL, TRANSDUCTION",
author = "Mauno Vihinen and D VETRIE and HS MANIAR and HD OCHS and QL ZHU and I VORECHOVSKY and ADB WEBSTER and LD NOTARANGELO and L NILSSON and JM SOWADSKI and CIE SMITH",
year = "1994",
doi = "10.1073/pnas.91.26.12803",
language = "English",
volume = "91",
pages = "12803--12807",
journal = "Proceedings of the National Academy of Sciences",
issn = "1091-6490",
publisher = "National Acad Sciences",
number = "26",

}