1zmf: Difference between revisions
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'''C domain of human cyclophilin-33(hcyp33)''' | {{Structure | ||
|PDB= 1zmf |SIZE=350|CAPTION= <scene name='initialview01'>1zmf</scene>, resolution 1.88Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''C domain of human cyclophilin-33(hcyp33)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZMF is a [ | 1ZMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZMF OCA]. | ||
==Reference== | ==Reference== | ||
1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase., Wang T, Yun CH, Gu SY, Chang WR, Liang DC, Biochem Biophys Res Commun. 2005 Aug 5;333(3):845-9. PMID:[http:// | 1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase., Wang T, Yun CH, Gu SY, Chang WR, Liang DC, Biochem Biophys Res Commun. 2005 Aug 5;333(3):845-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15963461 15963461] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: ppiase]] | [[Category: ppiase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:37:17 2008'' | ||
Revision as of 13:37, 20 March 2008
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| 1zmf, resolution 1.88Å | |||||||||||||
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| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
C domain of human cyclophilin-33(hcyp33)
Overview
Cyclophilins (CyPs) are a widespreading protein family in living organisms and possess the activity of peptidyl-prolyl cis-trans isomerase (PPIase), which is inhibited by cyclosporin A (CsA). The human nuclear cyclophilin (hCyP33) is the first protein which was found to contain two RNA binding domains at the amino-terminus and a PPIase domain at the carboxyl-terminus. We isolated the hCyP33 gene from the human hematopoietic stem/progenitor cells and expressed it in Escherichia coli, and determined the crystal structure of the C domain of hCyP33 at 1.88 A resolution. The core structure is a beta-barrel covered by two alpha-helices. Superposition of the structure of the C domain of hCyP33 with the structure of CypA suggests that the C domain contains PPIase active site which binds to CsA. Furthermore, C domain seems to be able to bind with the Gag-encoded capsid (CA) of HIV-1 and may affect the viral replication of HIV-1. A key residue of the active site is changed from Ala-103-CypA to Ser-239-hCyP33, which may affect the PPIase domain/substrates interactions.
About this Structure
1ZMF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase., Wang T, Yun CH, Gu SY, Chang WR, Liang DC, Biochem Biophys Res Commun. 2005 Aug 5;333(3):845-9. PMID:15963461
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