CRYSTAL-STRUCTURE OF THE RAG1 DIMERIZATION DOMAIN REVEALS MULTIPLE ZINC-BINDING MOTIFS INCLUDING A NOVEL ZINC BINUCLEAR CLUSTER

Authors
BELLON SF RODGERS KK SCHATZ DG COLEMAN JE STEITZ TA
Citation
Sf. Bellon et al., CRYSTAL-STRUCTURE OF THE RAG1 DIMERIZATION DOMAIN REVEALS MULTIPLE ZINC-BINDING MOTIFS INCLUDING A NOVEL ZINC BINUCLEAR CLUSTER, Nature structural biology, 4(7), 1997, pp. 586-591
Citations number
49
Categorie Soggetti
Biology,"Cell Biology
Journal title
Nature structural biology → ACNP
ISSN journal
10728368
Volume
4
Issue
7
Year of publication
1997
Pages
586 - 591
Database
ISI
SICI code
1072-8368(1997)4:7<586:COTRDD>2.0.ZU;2-Q
Abstract
The crystal structure of the dimerization domain of the V(D)J recombin ation-activating protein, RAG1, was solved using zinc anomalous scatte ring. 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 contain s a unique zinc binuclear cluster in place of a normally mononuclear z inc site in the RING finger. Together, four zinc ions help organize th e entire domain, including the two helices that form the dimer interfa ce.