MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES

被引：609

作者：

MEADOR, WE

MEANS, AR

QUIOCHO, FA

机构：

[1] BAYLOR COLL MED,HOWARD HUGHES MED INST,HOUSTON,TX 77030

[2] BAYLOR COLL MED,DEPT BIOCHEM,HOUSTON,TX 77030

[3] BAYLOR COLL MED,DEPT MOLEC PHYSIOL & BIOPHYS,HOUSTON,TX 77030

[4] DUKE UNIV,MED CTR,DEPT PHARMACOL,DURHAM,NC 27710

来源：

SCIENCE | 1993年 / 262卷 / 5140期

关键词：

D O I：

10.1126/science.8259515

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：

Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase IIalpha was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.

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页码：1718 / 1721

页数：4

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