Structural Basis for Protein Recognition by B30.2/SPRY Domains

Jae Sung Woo, Hye Young Suh, Sam Yong Park, Byung Ha Oh

Research output: Contribution to journalArticlepeer-review

103 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)967-976
Number of pages10
JournalMolecular Cell
Volume24
Issue number6
DOIs
Publication statusPublished - 2006 Dec 28
Externally publishedYes

Bibliographical note

Funding Information:
We thank Dr. S. Kim for the help with the analysis of human protein sequences. This study made use of the beam line NW12A at Photon Factory in Japan and was supported by Creative Research Initiatives (Center for Biomolecular Recognition) of MOST/KOSEF of Korea. J.-S.W. and H.-Y.S. were supported by the Brain Korea 21 Project.

Keywords

  • SIGNALING

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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