期刊
GENES & DEVELOPMENT
卷 17, 期 20, 页码 2508-2513出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1119403
关键词
Brain Tumor; Pumilio; mRNA translation; NHL domain; beta-propellor; crystal structure
资金
- NICHD NIH HHS [T32-HD-40372, T32 HD040372] Funding Source: Medline
- NIGMS NIH HHS [GM62947, R01 GM062947] Funding Source: Medline
- PHS HHS [G64726] Funding Source: Medline
The Brain Tumor (Brat) protein is recruited to the 3' untranslated region (UTR) of hunchback mRNA to regulate its translation. Recruitment is mediated by interactions between the Pumilio RNA-binding Puf repeats and the NHL domain of Brat, a conserved structural motif present in a large family of growth regulators. In this report, we describe the crystal structure of the Brat NHL domain and present a model of the Pumilio-Brat complex derived from in silico docking experiments and supported by mutational analysis of the protein-protein interface. A key feature of the model is recognition of the outer, convex surface of the Pumilio Puf domain by the top, electropositive face of the six-bladed Brat beta-propeller. In particular, an extended loop in Puf repeat 8 fits in the entrance to the central channel of the Brat beta-propeller. Together, these interactions are likely to be prototypic of the recruitment strategies of other NHL-containing proteins in development.
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