The tandem Src homology 2 domain of the Syk kinase: A molecular device that adapts to interphosphotyrosine distances

被引：38

作者：

Kumaran, S

Grucza, RA

Waksman, G

机构：

[1] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA

[2] Washington Univ, Sch Med, Dept Psychiat, St Louis, MO 63110 USA

[3] Univ London Birkbeck Coll, Sch Crystallog, London WC1E 7HX, England

[4] UCL, Dept Biochem & Mol Biol, London WC1E 6BT, England

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2003年 / 100卷 / 25期

关键词：

D O I：

10.1073/pnas.2432867100

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Conformational flexibility is important for protein function. However, information on the range of conformations accessible to macromolecules in the unbound state is often difficult to obtain. By using the model system of the tandem Src homology 2 domain (i.e., two adjacent Src homology 2 domains) of the Syk kinase, we report a method combining calorimetric and crystallographic measurements that reveals the preexistence of a conformational equilibrium in the unbound state, and that shows that this equilibrium is crucial for function.

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页码：14828 / 14833

页数：6

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