Publication Abstract from PubMed
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.
A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen.,Zong Y, Xu Y, Liang X, Keene DR, Hook A, Gurusiddappa S, Hook M, Narayana SV EMBO J. 2005 Dec 21;24(24):4224-36. Epub 2005 Dec 15. PMID:16362049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
