Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation

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• 作者：Elias J. Fernandez ; Jill Wilken ; Darren A. Thompson ; Stephen C. Peiper ; and Elias Lolis
• 刊名：Biochemistry
• 出版年：2000
• 出版时间：October 24, 2000
• 年：2000
• 卷：39
• 期：42
• 页码：12837 - 12844
• 全文大小：742K
• 年卷期：v.39,no.42(October 24, 2000)
• ISSN：1520-4995

文摘

Herpesvirus-8 macrophage inflammatory protein-II (vMIP-II) binds a uniquely wide spectrumof chemokine receptors. We report the X-ray structure of vMIP-II determined to 2.1 Å resolution. LikeRANTES, vMIP-II crystallizes as a dimer and displays the conventional chemokine tertiary fold. Wehave 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 epitopesidentified on RANTES to be involved in binding to CCR3 are mimicked on the eotaxin-1 and MCP-3surface. However, the surface topology of vMIP-II in these regions is markedly different. The resultspresented here indicate that the structural basis for interaction with the chemokine receptor CCR3 byvMIP-II is different from that for the physiological agonists eotaxin-1, RANTES, and MCP-3. Thesedifferences on vMIP-II may be a consequence of its broad-range receptor recognition capabilities.