1zmf
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(New page: 200px<br /> <applet load="1zmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zmf, resolution 1.88Å" /> '''C domain of human c...)
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Revision as of 18:30, 12 November 2007
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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. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 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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