Both proline-rich sequences in the TH region of Bruton's tyrosine kinase stabilize intermolecular interactions with the SH3 domain

被引：8

作者：

Hansson, H

Smith, CIE

Härd, T ^{[1
]}

机构：

[1] Royal Inst Technol, Dept Biotechnol, SCFAB, S-10691 Stockholm, Sweden

[2] Karolinska Inst, Novum, Dept Biosci, S-14157 Huddinge, Sweden

[3] Huddinge Univ Hosp, Karolinska Inst, Clin Res Ctr, S-14186 Huddinge, Sweden

来源：

FEBS LETTERS | 2001年 / 508卷 / 01期

关键词：

Bruton's tyrosine kinase; Src homology 3; dimerization; nuclear magnetic resonance; gel permeation chromatography; signal transduction;

D O I：

10.1016/S0014-5793(01)03018-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Tee homology (TH) region located N-terminal to the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk) contains two proline-rich SH3-binding sequences (PRRs). We have previously demonstrated that the TH region acts to stabilize intermolecular interactions in N-terminally extended SH3 (PRR-SH3) fragments. Here, we analyze six PRR-SH3 fragments with different proline-to-alanine substitutions in the two PRRs. Gel permeation chromatography and nuclear magnetic resonance spectroscopy show that both PRRs can stabilize self-association. This observation provides an explanation to why the TH region of Btk makes intermolecular interactions, whereas the corresponding interaction in the related Itk kinase with only one PRR, is intramolecular. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：11 / 15

页数：5

共 19 条

[11] MYRISTYLATION AND PALMITYLATION OF SRC FAMILY MEMBERS - THE FATS OF THE MATTER [J].