Barinka Cyril, Prahl Adam, Lubkowski Jacek
National Cancer Institute at Frederick, Center for Cancer Research, Frederick, MD 21702, USA.
Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):273-8. doi: 10.1107/S0907444907066164. Epub 2008 Feb 20.
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.
单核细胞趋化蛋白（MCPs）属于CC趋化因子家族，参与许多以单核细胞浸润为特征的（病理）生理过程，包括组织重塑、动脉粥样硬化和癌症转移。在此，报道了人单核细胞趋化蛋白4（MCP-4）在1.70 Å分辨率下精制的晶体结构，晶体学值R = 0.180，R free = 0.212。MCP-4的整体折叠结构揭示了CC趋化因子家族典型的三级结构特征。一个中央的三股反平行β-折叠在C端由一个重叠的α-螺旋侧翼，而分子的N端部分形成一个延伸环，该环通过两个二硫键Cys11-Cys35和Cys12-Cys51锚定到分子的其余部分。晶体堆积表明存在MCP-4二聚体，其二聚化界面与先前报道的MCP-1和MCP-2的X射线结构相似。
