Structure of μ-crystallin refined at 1.9- resolution and its ketimine reductase active site analysis

XU Xinlei LI Jian SUN Lihua XU Chunyan HE Jianhua

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Structure of μ-crystallin refined at 1.9- resolution and its ketimine reductase active site analysis

更新时间：2021-03-05

- Structure of μ-crystallin refined at 1.9- resolution and its ketimine reductase active site analysis
- NUCLEAR TECHNIQUES Vol. 35, Issue 10, (2012)
- 作者机构：
  
  中国科学院上海应用物理研究所
- 作者简介：
- 基金信息：
  
  国家自然科学基金(31100528);中国科学院知识创新工程领域前沿基金(O95501C061)资助
- DOI：
  CLC： O631.5
- Published：01 October 2012
- 稿件说明：
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[1]许新磊,李健,孙丽华,徐春艳,何建华.1.9分辨率μ-crystallin蛋白晶体结构及其酮亚胺还原酶活性位点分析[J].核技术,2012,35(10):721-727.

XU Xinlei LI Jian SUN Lihua XU Chunyan HE Jianhua. Structure of μ-crystallin refined at 1.9- resolution and its ketimine reductase active site analysis[J]. Nuclear techniques, 2012, 35(10): 721-727.
[1]许新磊,李健,孙丽华,徐春艳,何建华.1.9分辨率μ-crystallin蛋白晶体结构及其酮亚胺还原酶活性位点分析[J].核技术,2012,35(10):721-727. DOI：

XU Xinlei LI Jian SUN Lihua XU Chunyan HE Jianhua. Structure of μ-crystallin refined at 1.9- resolution and its ketimine reductase active site analysis[J]. Nuclear techniques, 2012, 35(10): 721-727. DOI：

摘要

采用不同的结晶条件生长了μ-crystallin晶体（CRYM）并解析了人源CRYM与NADPH复合物晶体结构（PDB code 2I99）

将分辨率由2.6提高至1.9

修正了2I99的结构。CRYM单体相较2I99结构少3个β折叠和一个310螺旋。NADPH Pro-R面具有多个保守位点可能参与酮亚胺还原酶活性

通过与同源蛋白OCD和AlaDH比对

推测了底物结合位点和催化位点。

Abstract

μ-crystallin

or CRYM

is an NADPH-dependent T3 binding protein in cytosol

has and is of pivotal roles in physiological regulation of thyroid hormone action in vivo.Human CRYM has been identified as ketimine reductase and potential regulated by T3.In this paper

the crystal structure of human CRYM is resolved at 1.9 and compared with 2I99.The differences between CRYM monomer and 2I99 are three β sheet and two 310helixes.The dimerization domain in CRYM presents a cluster of conserved residues side-chain over the Pro-R face of the cofactor NADPH.Compared the overall structure of CRYM with its structural homologs P.putida OCD and A.fulgidus AlaDH

we can deduce ketimine binding site and catalytic site in human CRYM.

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何建华

胡小健

2 TANG Lin 1 HU Xiaojian3 HE Jianhua 1 1

2 SUN Lihua1

2 YU Feng1

XU Chunyan1

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CHEN Zhenping1 LI Xigui2 SU Yuling1 XUE Yuncai1 LIU Haizeng1 GONG Shicheng1 ZHAO Jingxun1 1

Related Institution

复旦大学生理学和生物物理学系

中国科学院研究生院

Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China) 2

河南师范大学物理系

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