A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography

Title:A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography

Volume: 22 Issue: 3

Author(s): Christophe Guillon, Ulrick Mavoungou Bigouagou, Christelle Folio, Pascale Jeannin, Yves Delneste and Patrice Gouet

Affiliation:

Keywords: Acute phase, C-reactive protein, CRP, decamer, innate immunity, pentraxin, structure, X-ray crystallography, zinc.

Abstract: Human C-reactive protein (CRP) is an acute phase protein, which harbours both host defence and scavenging properties. In this study, we obtained two new crystal forms of CRP, where CRP forms a symmetric, staggered dimer of pentamers. In one of these structures, obtained in the presence of HIV-1 Tat protein, this dimer of pentamers is stabilized by two zinc ions trapped within a cleft of the effector face of CRP. These two decameric interfaces involve complementary surfaces of CRP pentamers and bury a large area of ~2000 Ų per pentamer, suggesting a biological role of this interface. These two novel decameric interfaces and the involvement of zinc might have important consequences in the understanding of CRP biological functions.

Cite this article as:

Guillon Christophe, Bigouagou Mavoungou Ulrick, Folio Christelle, Jeannin Pascale, Delneste Yves and Gouet Patrice, A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography, Protein & Peptide Letters 2015; 22 (3) . https://dx.doi.org/10.2174/0929866522666141231111226