Crystal Structure of Human Monocyte Chemoattractant Protein 4 (MCP-4/CCL13)
[CCL13_HUMAN] Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. Signals through CCR2B and CCR3 receptors. Plays a role in the accumulation of leukocytes at both sides of allergic and non-allergic inflammation. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. May play a role in the monocyte attraction in tissues chronically exposed to exogenous pathogens.
Publication Abstract from PubMed
Monocyte chemoattractant proteins (MCPs) belong to the CC chemokine family and are involved in many (patho)physiological processes characterized by mononuclear cell infiltration, including tissue remodeling, atherosclerosis and cancer metastasis. Here, the crystal structure of human monocyte chemoattractant protein 4 (MCP-4) refined at 1.70 A resolution is reported with crystallographic values R = 0.180 and R free = 0.212. The overall MCP-4 fold reveals the typical tertiary features of the CC chemokine family. A central three-stranded antiparallel beta-sheet is C-terminally flanked by an overlaying alpha-helix, while the N-terminal part of the molecule forms an extended loop that is anchored to the rest of the molecule via two disulfide bridges, Cys11-Cys35 and Cys12-Cys51. The crystal packing suggests the existence of MCP-4 dimers with a dimerization interface similar to those previously reported for the X-ray structures of MCP-1 and MCP-2.
Structure of human monocyte chemoattractant protein 4 (MCP-4/CCL13).,Barinka C, Prahl A, Lubkowski J Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):273-8. Epub 2008, Feb 20. PMID:18323622
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.