1CM9: Crystal Structure Of Viral Macrophage Inflammatory Protein-Ii

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.
PDB ID: 1CM9Download
MMDB ID: 15750
PDB Deposition Date: 1999/5/19
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 1CM9: dimeric; determined by author and by software (PISA)
Molecular Components in 1CM9
Label Count Molecule
Proteins (2 molecules)
Protein (Viral Macrophage Inflammatory Protein-ii)(Gene symbol: K4)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB