3PVN

Triclinic form of Human C-Reactive Protein in complex with Zinc

Summary for 3PVN

• Entry DOI: 10.2210/pdb3pvn/pdb
• Related: 1LJ7 3PVO
• Descriptor: C-reactive protein, CALCIUM ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: pentraxin family, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02741
• Total number of polymer chains: 20
• Total formula weight: 463290.95

Authors

Guillon, C.,Mavoungou Bigouagou, U.,Jeannin, P.,Delneste, Y.,Gouet, P. (deposition date: 2010-12-07, release date: 2012-01-11, Last modification date: 2024-10-30)

Primary citation

Guillon, C.,Bigouagou, U.M.,Folio, C.,Jeannin, P.,Delneste, Y.,Gouet, P.
A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography.
Protein Pept.Lett., 22:248-255, 2014

PubMed 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 Å(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.

PubMed: 25552313

Experimental method

X-RAY DIFFRACTION (1.98 Å)