The crystal structure of human protein ¦Á1M reveals a chromophore-binding site and two putative protein-protein interfaces

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• 作者：Yangli Zhang ; Zengqiang Gao ; Zhen Guo ; Hongpeng Zhang ; Zhenzhen Zhang ; Miao Luo ; Haifeng Hou ; Ailong Huang ; Yuhui Dong ; Deqiang Wang
• 关键词：¦Á1-Microglobulin ; Crystal structure ; Homodimer ; Chromophore ; Interface
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2013
• 出版时间：27 September, 2013
• 年：2013
• 卷：439
• 期：3
• 页码：346-350
• 全文大小：1348 K

文摘

Lipocalin ¦Á1-microglobulin (¦Á1M) is a conserved glycoprotein present in plasma and in the interstitial fluids of all tissues. ¦Á1M is linked to a heterogeneous yellow-brown chromophore of unknown structure, and interacts with several target proteins, including ¦Á1-inhibitor-3, fibronectin, prothrombin and albumin. To date, there is little knowledge about the interaction sites between ¦Á1M and its partners. Here, we report the crystal structure of the human ¦Á1M. Due to the crystallization occurring in a low ionic strength solution, the unidentified chromophore with heavy electron density is observed at a hydrophobic inner tube of ¦Á1M. In addition, two conserved surface regions of ¦Á1M are proposed as putative protein-protein interface sites. Further study is needed to unravel the detailed information about the interaction between ¦Á1M and its partners.