1ncv

From Proteopedia

Revision as of 16:14, 12 November 2007

DETERMINATION CC-CHEMOKINE MCP-3, NMR, 7 STRUCTURES

Overview

MCP-3 is a beta chemokine consisting of 76 amino acid residues. It has, been described to be involved in the activation of all leukocytic cells, activation mediated by the presence of multiple binding sites on the, target cells. Its three-dimensional structure has been studied by making, use of two-dimensional 1H NMR spectroscopy. MCP-3 exhibits the same, monomeric structure as the other chemokines, i.e., a three-stranded, antiparallel beta sheet covered on one face by an alpha helix. Although it, belongs to the same subfamily as RANTES (Chung et al., 1995; Faitbrother, et al., 1994) and hMIP-1beta (Lodi et al., 1994), the MCP-3 dimer is, folded like IL-8 with the so-called alphabeta sandwich structural motif., Structural and sequence analysis gives clear indications suggesting that, the other MCP chemokines may have the same quaternary structure, contrary, to the other beta chemokines.

About this Structure

1NCV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy., Meunier S, Bernassau JM, Guillemot JC, Ferrara P, Darbon H, Biochemistry. 1997 Apr 15;36(15):4412-22. PMID:9109648

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