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Title: The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein–protein interfaces

Abstract

Highlights: •We determined the first structure of human α1M with heavy electron density of the chromophore. •We proposed a new structural model of the chromophore. •We first revealed that the two conserved surface regions of α1M are proposed as putative protein–protein interface sites. -- Abstract: Lipocalin α1-microglobulin (α1M) is a conserved glycoprotein present in plasma and in the interstitial fluids of all tissues. α1M is linked to a heterogeneous yellow–brown chromophore of unknown structure, and interacts with several target proteins, including α1-inhibitor-3, fibronectin, prothrombin and albumin. To date, there is little knowledge about the interaction sites between α1M and its partners. Here, we report the crystal structure of the human α1M. 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 α1M. In addition, two conserved surface regions of α1M are proposed as putative protein–protein interface sites. Further study is needed to unravel the detailed information about the interaction between α1M and its partners.

Authors:
 [1];  [2]; ;  [1];  [1];  [3];  [2];  [1];  [2];  [1]
  1. Key Laboratory of Molecular Biology on Infectious Disease, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016 (China)
  2. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, 19B Yuquan Road, Beijing 100039 (China)
  3. College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016 (China)
Publication Date:
OSTI Identifier:
22242111
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 439; Journal Issue: 3; Other Information: Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 60 APPLIED LIFE SCIENCES; ALBUMINS; ANIMAL TISSUES; CRYSTAL STRUCTURE; CRYSTALLIZATION; ELECTRON DENSITY; GLYCOPROTEINS; HUMAN POPULATIONS; INTERFACES; PROTHROMBIN; STRUCTURAL MODELS

Citation Formats

Zhang, Yangli, College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, The Center for Clinical Molecular Medical detection of Chongqing, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, Gao, Zengqiang, Guo, Zhen, Zhang, Hongpeng, College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, Zhang, Zhenzhen, Luo, Miao, Hou, Haifeng, Huang, Ailong, Dong, Yuhui, Wang, Deqiang, and College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016. The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein–protein interfaces. United States: N. p., 2013. Web. doi:10.1016/J.BBRC.2013.08.084.
Zhang, Yangli, College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, The Center for Clinical Molecular Medical detection of Chongqing, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, Gao, Zengqiang, Guo, Zhen, Zhang, Hongpeng, College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, Zhang, Zhenzhen, Luo, Miao, Hou, Haifeng, Huang, Ailong, Dong, Yuhui, Wang, Deqiang, & College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016. The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein–protein interfaces. United States. https://doi.org/10.1016/J.BBRC.2013.08.084
Zhang, Yangli, College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, The Center for Clinical Molecular Medical detection of Chongqing, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, Gao, Zengqiang, Guo, Zhen, Zhang, Hongpeng, College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, Zhang, Zhenzhen, Luo, Miao, Hou, Haifeng, Huang, Ailong, Dong, Yuhui, Wang, Deqiang, and College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016. 2013. "The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein–protein interfaces". United States. https://doi.org/10.1016/J.BBRC.2013.08.084.
@article{osti_22242111,
title = {The crystal structure of human protein α1M reveals a chromophore-binding site and two putative protein–protein interfaces},
author = {Zhang, Yangli and College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016 and The Center for Clinical Molecular Medical detection of Chongqing, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016 and Gao, Zengqiang and Guo, Zhen and Zhang, Hongpeng and College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016 and Zhang, Zhenzhen and Luo, Miao and Hou, Haifeng and Huang, Ailong and Dong, Yuhui and Wang, Deqiang and College of Laboratory Medicine, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016},
abstractNote = {Highlights: •We determined the first structure of human α1M with heavy electron density of the chromophore. •We proposed a new structural model of the chromophore. •We first revealed that the two conserved surface regions of α1M are proposed as putative protein–protein interface sites. -- Abstract: Lipocalin α1-microglobulin (α1M) is a conserved glycoprotein present in plasma and in the interstitial fluids of all tissues. α1M is linked to a heterogeneous yellow–brown chromophore of unknown structure, and interacts with several target proteins, including α1-inhibitor-3, fibronectin, prothrombin and albumin. To date, there is little knowledge about the interaction sites between α1M and its partners. Here, we report the crystal structure of the human α1M. 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 α1M. In addition, two conserved surface regions of α1M are proposed as putative protein–protein interface sites. Further study is needed to unravel the detailed information about the interaction between α1M and its partners.},
doi = {10.1016/J.BBRC.2013.08.084},
url = {https://www.osti.gov/biblio/22242111}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 439,
place = {United States},
year = {Fri Sep 27 00:00:00 EDT 2013},
month = {Fri Sep 27 00:00:00 EDT 2013}
}