2RA4

Crystal Structure of Human Monocyte Chemoattractant Protein 4 (MCP-4/CCL13)

Summary for 2RA4

• Entry DOI: 10.2210/pdb2ra4/pdb
• Descriptor: Small-inducible cytokine A13, SULFATE ION, trifluoroacetic acid, ... (4 entities in total)
• Functional Keywords: ccl13, mcp-4, cc chemokine family, chemotaxis, monocytes, cytokine, inflammatory response, pyrrolidone carboxylic acid, secreted
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q99616
• Total number of polymer chains: 2
• Total formula weight: 18185.19

Authors

Lubkowski, J.,Barinka, C. (deposition date: 2007-09-14, release date: 2008-03-18, Last modification date: 2024-10-30)

Primary citation

Barinka, C.,Prahl, A.,Lubkowski, J.
Structure of human monocyte chemoattractant protein 4 (MCP-4/CCL13).
Acta Crystallogr.,Sect.D, 64:273-278, 2008

PubMed Abstract: 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.

PubMed: 18323622
DOI: 10.1107/S0907444907066164

Experimental method

X-RAY DIFFRACTION (1.7 Å)