Stability and peptide binding specificity of Btk SH2 domain: molecular basis for X-linked agammaglobulinemia.

@article{Tzeng2000StabilityAP,
  title={Stability and peptide binding specificity of Btk SH2 domain: molecular basis for X-linked agammaglobulinemia.},
  author={S R Tzeng and M T Pai and F D Lung and Cindy W Wu and Peter P. Roller and Benfang Lei and C J Wei and S C Tu and Shengfu Chen and Wen-Jue Soong and Jyin Wen Cheng},
  journal={Protein science : a publication of the Protein Society},
  year={2000},
  volume={9 12},
  pages={2377-85}
}
X-linked agammaglobulinemia (XLA) is caused by mutations in the Bruton's tyrosine kinase (Btk). The absence of functional Btk leads to failure of B-cell development that incapacitates antibody production in XLA patients leading to recurrent bacterial infections. Btk SH2 domain is essential for phospholipase C-gamma phosphorylation, and mutations in this domain were shown to cause XLA. Recently, the B-cell linker protein (BLNK) was found to interact with the SH2 domain of Btk, and this… CONTINUE READING

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