Solution Structure of the SH3 Domain from Bruton's Tyrosine Kinase †,‡
✍ Scribed by Hansson, Henrik; Mattsson, Pekka T.; Allard, Peter; Haapaniemi, Pekka; Vihinen, Mauno; Smith, C. I. Edvard; Härd, Torleif
- Book ID
- 127353765
- Publisher
- American Chemical Society
- Year
- 1998
- Tongue
- English
- Weight
- 222 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0006-2960
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Bruton's tyrosine kinase (BTK) plays an important role in B cell development. Deletion of C-terminal14 amino acids of the SH3 domain of BTK results in X-linked a g ammaglobulinemia ( X U ) , an inherited disease. We report here on the stability and folding of SH3 domain of BTK. Peptides correspondin
X-linked agammaglobulinemia (XLA), an inherited disease, is caused by mutations in the Bruton's tyrosine kinase (BTK). The absence of functional BTK leads to failure of B-cell differentiation; this incapacitates antibody production in XLA patients, who suffer from recurrent, sometimes lethal, bacter