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

Yinong Zong, Yi Xu, Xiaowen Liang, Douglas R. Keene, Agneta Höök, Shivasankarappa Gurusiddappa, Magnus Höök, Sthanam V.L. Narayana

Research output: Contribution to journalArticlepeer-review

194 Scopus citations


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 interdomain 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.

Original languageEnglish (US)
Pages (from-to)4224-4236
Number of pages13
JournalEMBO Journal
Issue number24
StatePublished - Dec 21 2005


  • Bacterial adhesion
  • Collagen binding
  • Protein-protein
  • Surface proteins

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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