Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster

被引：125

作者：

Bellon, SF ^{[1
]}

Rodgers, KK ^{[1
]}

Schatz, DG ^{[1
]}

Coleman, JE ^{[1
]}

Steitz, TA ^{[1
]}

机构：

[1] YALE UNIV, SCH MED, HOWARD HUGHES MED INST, IMMUNOL SECT, NEW HAVEN, CT 06520 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 07期

关键词：

D O I：

10.1038/nsb0797-586

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 crystal structure of the dimerization domain of the V(D)J recombination-activating protein, RAG1, was solved using zinc anomalous scattering. The structure reveals an unusual combination of multi-class zinc-binding motifs, including a zinc RING finger and a C2H2 zinc finger, that together form a single structural domain. The domain also contains a unique zinc binuclear cluster in place of a normally mononuclear zinc site in the RING finger. Together, four zinc ions help organize the entire domain, including the two helices that form the dimer interface.

引用

页码：586 / 591

页数：6

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