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

作者：Guillon Christophe^*; Bigouagou Ulrick Mavoungou; Folio Christelle; Jeannin Pascale; Delneste Yves; Gouet Patrice

来源：Protein and Peptide Letters, 2015, 22(3): 248-255.

DOI：10.2174/0929866522666141231111226

• Acute phase
• C-reactive protein
• CRP
• decamer
• innate immunity
• pentraxin
• structure
• X-ray crystallography
• zinc

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 similar to 2000 angstrom(2) 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.

• 出版日期2015