Structural basis for protein recognition by B30.2/SPRY domains
SCIE
SCOPUS
- Title
- Structural basis for protein recognition by B30.2/SPRY domains
- Authors
- Woo, JS; Suh, HY; Park, SY; Oh, BH
- Date Issued
- 2006-12-28
- Publisher
- CELL PRESS
- Abstract
- B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.
- Keywords
- UBIQUITIN LIGASES; SOCS-BOX; INTERACTION MAP; SPRY-DOMAIN; CELL-CYCLE; RESTRICTION; DESTRUCTION; SPECIFICITY; APOPTOSIS; PRIMATES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/23628
- DOI
- 10.1016/j.molcel.2006.11.009
- ISSN
- 1097-2765
- Article Type
- Article
- Citation
- MOLECULAR CELL, vol. 24, no. 6, page. 967 - 976, 2006-12-28
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