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Intermolecular interactions between the SH3 domain and the proline‐rich TH region of Bruton's tyrosine kinase
Author(s) -
Hansson Henrik,
Okoh Michael P,
Smith C.I.Edvard,
Vihinen Mauno,
Härd Torleif
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02438-8
Subject(s) - bruton's tyrosine kinase , sh3 domain , dimer , chemistry , proto oncogene tyrosine protein kinase src , tyrosine , tyrosine kinase , proline , intermolecular force , biophysics , stereochemistry , biochemistry , kinase , biology , molecule , amino acid , signal transduction , organic chemistry
The SH3 domain of Bruton's tyrosine kinase (Btk) is preceded by the Tec homology (TH) region containing proline‐rich sequences. We have studied a protein fragment containing both the Btk SH3 domain and the proline‐rich sequences of the TH region (PRR‐SH3). Intermolecular NMR cross‐relaxation measurements, gel permeation chromatography profiles, titrations with proline‐rich peptides, and 15 N NMR relaxation measurements are all consistent with a monomer–dimer equilibrium with a dissociation constant on the order of 60 μM. The intermolecular interactions do, at least in part, involve proline‐rich sequences in the TH region. This behavior of Btk PRR‐SH3 may have implications for the functional action of Btk.