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EMBO J. 2005 Dec 21;24(24):4224-36. Epub 2005 Dec 15.

A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen.

Author information

1
School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Erratum in

  • EMBO J. 2006 Feb 22;25(4):921.

Abstract

The structural basis for the association of eukaryotic and prokaryotic protein receptors and their triple-helical collagen ligand remains poorly understood. Here, we present the crystal structures of a high affinity subsegment of the Staphylococcus aureus collagen-binding CNA as an apo-protein and in complex with a synthetic collagen-like triple helical peptide. The apo-protein structure is composed of two subdomains (N1 and N2), each adopting a variant IgG-fold, and a long linker that connects N1 and N2. The structure is stabilized by hydrophobic inter-domain interactions and by the N2 C-terminal extension that complements a beta-sheet on N1. In the ligand complex, the collagen-like peptide penetrates through a spherical hole formed by the two subdomains and the N1-N2 linker. Based on these two structures we propose a dynamic, multistep binding model, called the 'Collagen Hug' that is uniquely designed to allow multidomain collagen binding proteins to bind their extended rope-like ligand.

PMID:
16362049
PMCID:
PMC1356329
DOI:
10.1038/sj.emboj.7600888
[Indexed for MEDLINE]
Free PMC Article

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