1xyh
From Proteopedia
(New page: 200px<br /> <applet load="1xyh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xyh, resolution 2.60Å" /> '''Crystal Structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1xyh.gif|left|200px]]<br /> | + | [[Image:1xyh.gif|left|200px]]<br /><applet load="1xyh" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xyh" size=" | + | |
caption="1xyh, resolution 2.60Å" /> | caption="1xyh, resolution 2.60Å" /> | ||
'''Crystal Structure of Recombinant Human Cyclophilin J'''<br /> | '''Crystal Structure of Recombinant Human Cyclophilin J'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cyclophilins (CyPs) are a large class of highly conserved ubiquitous | + | Cyclophilins (CyPs) are a large class of highly conserved ubiquitous peptidyl-prolyl cis-trans isomerases. CyPs have also been identified as being a specific receptor for the immunosuppressive drug cyclosporin A and are involved in a variety of biological functions. CyPJ is a novel member of the CyP family and human CyPJ (hCyPJ) is the protein encoded by a cyclophilin-like gene from human foetal brain, which shows 50% sequence identity to human cyclophilin A (hCyPA). Recombinant hCyPJ was expressed in Escherichia coli and purified. The three-dimensional structure of hCyPJ has been determined by molecular replacement using the hCyPA structure as the search model and has been refined at 2.6 angstroms resolution. The hCyPJ molecule contains four helices and one beta-barrel composed of eight antiparallel beta-strands. The overall secondary and tertiary structures of hCyPJ are similar to those of hCyPA, but hCyPJ contains an additional disulfide bridge and four segments with conformations that are strikingly different from those of hCyPA. His43 and Gln52 of hCyPJ are expected to be the active sites based on sequence alignment with hCyPA. The hCyPJ structure shows a conserved water molecule close to His43 and Gln52 which appears to support the solvent-assisted mechanism. |
==About this Structure== | ==About this Structure== | ||
| - | 1XYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http:// | + | 1XYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYH OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Huang, C | + | [[Category: Huang, C Q.]] |
| - | [[Category: Huang, L | + | [[Category: Huang, L L.]] |
| - | [[Category: Xia, Z | + | [[Category: Xia, Z X.]] |
[[Category: Yu, L.]] | [[Category: Yu, L.]] | ||
| - | [[Category: Zhao, X | + | [[Category: Zhao, X M.]] |
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: cyclophilin j]] | [[Category: cyclophilin j]] | ||
| Line 25: | Line 24: | ||
[[Category: helix]] | [[Category: helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:59 2008'' |
Revision as of 13:59, 21 February 2008
|
Crystal Structure of Recombinant Human Cyclophilin J
Overview
Cyclophilins (CyPs) are a large class of highly conserved ubiquitous peptidyl-prolyl cis-trans isomerases. CyPs have also been identified as being a specific receptor for the immunosuppressive drug cyclosporin A and are involved in a variety of biological functions. CyPJ is a novel member of the CyP family and human CyPJ (hCyPJ) is the protein encoded by a cyclophilin-like gene from human foetal brain, which shows 50% sequence identity to human cyclophilin A (hCyPA). Recombinant hCyPJ was expressed in Escherichia coli and purified. The three-dimensional structure of hCyPJ has been determined by molecular replacement using the hCyPA structure as the search model and has been refined at 2.6 angstroms resolution. The hCyPJ molecule contains four helices and one beta-barrel composed of eight antiparallel beta-strands. The overall secondary and tertiary structures of hCyPJ are similar to those of hCyPA, but hCyPJ contains an additional disulfide bridge and four segments with conformations that are strikingly different from those of hCyPA. His43 and Gln52 of hCyPJ are expected to be the active sites based on sequence alignment with hCyPA. The hCyPJ structure shows a conserved water molecule close to His43 and Gln52 which appears to support the solvent-assisted mechanism.
About this Structure
1XYH is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family., Huang LL, Zhao XM, Huang CQ, Yu L, Xia ZX, Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):316-21. Epub 2005, Feb 24. PMID:15735342
Page seeded by OCA on Thu Feb 21 15:59:59 2008
