A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography - Archive ouverte HAL Access content directly
Journal Articles Protein and Peptide Letters Year : 2015

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

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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 Å2 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.

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hal-01392233 , version 1 (04-11-2016)

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Christophe Guillon, Ulrick Bigouagou, Christelle Folio, Pascale Jeannin, Yves Delneste, et al.. A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography. Protein and Peptide Letters, 2015, 22 (3), pp.248 - 255. ⟨10.2174/0929866522666141231111226⟩. ⟨hal-01392233⟩
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