Structure and dynamic regulation of Src-family kinases

被引：163

作者：

Engen, J. R. ^{[2
,3
]}

Wales, T. E. ^{[2
,3
]}

Hochrein, J. M. ^{[4
]}

Meyn, M. A., III ^{[1
]}

Ozkan, S. Banu ^{[5
]}

Bahar, I. ^{[6
]}

Smithgall, T. E. ^{[1
]}

机构：

[1] Univ Pittsburgh, Dept Microbiol & Mol Genet, Sch Med, Pittsburgh, PA 15261 USA

[2] Northeastern Univ, Dept Chem & Chem Biol, Boston, MA 02115 USA

[3] Northeastern Univ, Barnett Inst Chem & Biol Anal, Boston, MA 02115 USA

[4] Sandia Natl Labs, Mat Reliabil Dept, Albuquerque, NM 87185 USA

[5] Arizona State Univ, Dept Phys, Ctr Biol Phys, Tempe, AZ 85287 USA

[6] Univ Pittsburgh, Dept Computat Biol, Sch Med, Pittsburgh, PA 15261 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2008年 / 65卷 / 19期

基金：

美国国家卫生研究院;

关键词：

Src-family kinases; SH3; domain; SH2; hydrogen exchange mass spectrometry; Gaussian Network Model;

D O I：

10.1007/s00018-008-8122-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Src-family kinases are modular signaling proteins involved in a diverse array of cellular processes. All members of the Src family share the same domain organization, with modular SH3, SH2 and kinase domains followed by a C-terminal negative regulatory tail. X-ray crystallographic analyses of several Src family members have revealed critical roles for the SH3 and SH2 domains in the down-regulation of the kinase domain. This review focuses on biological, biophysical, and computational studies that reveal conformationally distinct active states within this unique kinase family.

引用

页码：3058 / 3073

页数：16

共 91 条

[1]

Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein [J].

Arold, ST ;

Bauer, AS .

TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (06) :356-363

[2]

The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases [J].

Arold, ST ;

Ulmer, TS ;

Mulhern, TD ;

Werner, JM ;

Ladbury, JE ;

Campbell, ID ;

Noble, MEM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (20) :17199-17205

[3]

Vibrational dynamics of folded proteins: Significance of slow and fast motions in relation to function and stability [J].

Bahar, I ;

Atilgan, AR ;

Demirel, MC ;

Erman, B .

PHYSICAL REVIEW LETTERS, 1998, 80 (12) :2733-2736

[4]

Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential [J].

Bahar, I ;

Atilgan, AR ;

Erman, B .

FOLDING & DESIGN, 1997, 2 (03) :173-181

[5]

Intrinsic dynamics of enzymes in the unbound state and, relation to allosteric regulation [J].

Bahar, Ivet ;

Chennubhotla, Chakra ;

Tobi, Dror .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 2007, 17 (06) :633-640

[6]

THE PRODUCT OF THE HERPESVIRUS-SAIMIRI OPEN READING FRAME-1 (TIP) INTERACTS WITH T-CELL-SPECIFIC KINASE P56(LCK) IN TRANSFORMED-CELLS [J].

BIESINGER, B ;

TSYGANKOV, AY ;

FICKENSCHER, H ;

EMMRICH, F ;

FLECKENSTEIN, B ;

BOLEN, JB ;

BROKER, BM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (09) :4729-4734

[7]

Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases [J].

Boonyaratanakornkit, V ;

Scott, MP ;

Ribon, V ;

Sherman, L ;

Anderson, SM ;

Maller, JL ;

Miller, WT ;

Edwards, DP .

MOLECULAR CELL, 2001, 8 (02) :269-280

[8]

SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1 [J].

Briggs, SD ;

Sharkey, M ;

Stevenson, M ;

Smithgall, TE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (29) :17899-17902

[9]

THE RAS GTPASE-ACTIVATING PROTEIN (GAP) IS AN SH3 DOMAIN-BINDING PROTEIN AND SUBSTRATE FOR THE SRC-RELATED TYROSINE KINASE, HCK [J].

BRIGGS, SD ;

BRYANT, SS ;

JOVE, R ;

SANDERSON, SD ;

SMITHGALL, TE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (24) :14718-14724

[10]

SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts [J].

Briggs, SD ;

Smithgall, TE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (37) :26579-26583

← 1 2 3 4 5 6 7 8 9 10 →