Dynamics in multi-domain protein recognition of RNA

被引：94

作者：

Mackereth, Cameron D. ^{[1
,2
]}

Sattler, Michael ^{[3
,4
,5
]}

机构：

[1] INSERM, U869, Inst Europeen Chim & Biol, F-33607 Pessac, France

[2] Univ Bordeaux, F-33607 Pessac, France

[3] Helmholtz Zentrum Munchen, Inst Struct Eliol, D-85764 Neuherberg, Germany

[4] Tech Univ Munich, Biomol NMR, D-85747 Garching, Germany

[5] Tech Univ Munich, Ctr Integrated Prot Sci Munich, Dept Chem, D-85747 Garching, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2012年 / 22卷 / 03期

关键词：

MAGNETIC-RESONANCE-SPECTROSCOPY; MOLECULAR-WEIGHT PROTEINS; EXPORT FACTOR TAP; X-RAY-SCATTERING; STRUCTURAL BASIS; NMR-SPECTROSCOPY; BINDING PROTEINS; COMPLEX REVEALS; CONFORMATIONAL SELECTION; SPLICING REGULATION;

D O I：

10.1016/j.sbi.2012.03.013

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：

Protein-RNA interactions play essential roles in gene regulation and RNA metabolism. While high-resolution structures have revealed principles of RNA recognition by individual RNA binding domains (RBDs), the presence of multiple RBDs in many eukaryotic proteins suggests additional modes of RNA recognition by combination and cooperation of these interactions. Recent structures, together with biochemical and biophysical studies have revealed novel principles of RNA recognition by multi-domain proteins. These examples highlight an important role for dynamics in RNA recognition, with mechanisms including fly-casting and conformational selection, and advocate the use of solution techniques for their analysis.

引用

页码：287 / 296

页数：10

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