1CM9

CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II

Summary for 1CM9

• Entry DOI: 10.2210/pdb1cm9/pdb
• Descriptor: PROTEIN (VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II) (2 entities in total)
• Functional Keywords: chemokine, herpesvirus-8, karposi's sarcoma
• Biological source: Human herpesvirus 8
• Cellular location: Secreted: Q98157
• Total number of polymer chains: 2
• Total formula weight: 16925.60

Authors

Fernandez, E.J.,Lolis, E. (deposition date: 1999-05-19, release date: 1999-06-24, Last modification date: 2024-11-20)

Primary citation

Fernandez, E.J.,Wilken, J.,Thompson, D.A.,Peiper, S.C.,Lolis, E.
Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation.
Biochemistry, 39:12837-12844, 2000

PubMed Abstract: Herpesvirus-8 macrophage inflammatory protein-II (vMIP-II) binds a uniquely wide spectrum of chemokine receptors. We report the X-ray structure of vMIP-II determined to 2.1 A resolution. Like RANTES, vMIP-II crystallizes as a dimer and displays the conventional chemokine tertiary fold. We have compared the surface topology and electrostatic potential of vMIP-II to those of eotaxin-1, RANTES, and MCP-3, three CCR3 physiological agonists with known three-dimensional structures. Surface epitopes identified on RANTES to be involved in binding to CCR3 are mimicked on the eotaxin-1 and MCP-3 surface. However, the surface topology of vMIP-II in these regions is markedly different. The results presented here indicate that the structural basis for interaction with the chemokine receptor CCR3 by vMIP-II is different from that for the physiological agonists eotaxin-1, RANTES, and MCP-3. These differences on vMIP-II may be a consequence of its broad-range receptor recognition capabilities.

PubMed: 11041848
DOI: 10.1021/bi001166f

Experimental method

X-RAY DIFFRACTION (2.1 Å)