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1zmf

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[[Image:1zmf.gif|left|200px]]<br /><applet load="1zmf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zmf, resolution 1.88&Aring;" />
 
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'''C domain of human cyclophilin-33(hcyp33)'''<br />
 
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==Overview==
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==C domain of human cyclophilin-33(hcyp33)==
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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.
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<StructureSection load='1zmf' size='340' side='right'caption='[[1zmf]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zmf]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZMF FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zmf OCA], [https://pdbe.org/1zmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zmf RCSB], [https://www.ebi.ac.uk/pdbsum/1zmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zmf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPIE_HUMAN PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zm/1zmf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zmf ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ZMF 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=1ZMF OCA].
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15963461 15963461]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chang W-R]]
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[[Category: Chang, W R.]]
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[[Category: Gu S-Y]]
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[[Category: Gu, S Y.]]
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[[Category: Liang D-C]]
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[[Category: Liang, D C.]]
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[[Category: Wang T]]
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[[Category: Wang, T.]]
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[[Category: Yun C-H]]
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[[Category: Yun, C H.]]
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[[Category: human cyclophilin-33]]
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[[Category: ppiase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:59 2008''
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Current revision

C domain of human cyclophilin-33(hcyp33)

PDB ID 1zmf

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