NDLI: A ‘Collagen Hug' Model for Staphylococcus aureus CNA binding to collagen

Content Provider	PubMed Central
Author	Zong, Yinong Xu, Yi Liang, Xiaowen Keene, Douglas R. Höök, Agneta Gurusiddappa, Shivasankarappa Magnus, Höök Narayana, Sthanam V. L.
Copyright Year	2005
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 β-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.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7600888
Ending Page	4236
Page Count	13
Starting Page	4224
File Format	PDF
ISSN	02614189
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	24
Volume Number	24
Language	English
Publisher	Nature Publishing Group
Publisher Date	2005-12-21
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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