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New page: left|200px<br /> <applet load="1mzw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mzw, resolution 2.0Å" /> '''Crystal structure of...
 
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[[Image:1mzw.gif|left|200px]]<br />
<applet load="1mzw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mzw, resolution 2.0&Aring;" />
'''Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide'''<br />


==Overview==
==Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide==
The spliceosomal cyclophilin H is a specific component of the human U4/U6, small nuclear ribonucleoprotein particle, interacting with homologous, sequences in the proteins U4/U6-60K and hPrp18 during pre-mRNA splicing., We determined the crystal structure of the complex comprising cyclophilin, H and the cognate domain of U4/U6-60K. The 31 amino acid fragment of, U4/U6-60K is bound to a region remote from the cyclophilin active site., Residues Ile118-Phe121 of U4/U6-60K expand the central beta-sheet of, cyclophilin H and the side-chain of Phe121 inserts into a hydrophobic, cavity. Concomitantly, in the crystal the cyclophilin H active site is, occupied by the N terminus of a neighboring cyclophilin H molecule in a, substrate-like manner, indicating the capacity of joint binding to a, substrate and to U4/U6-60K. Free and complexed cyclophilin H have, virtually identical conformations suggesting that the U4/U6-60K binding, site is pre-shaped and the peptidyl-prolyl-cis/trans isomerase activity is, unaffected by complex formation. The complex defines a novel, protein-protein interaction mode for a cyclophilin, allowing cyclophilin H, to mediate interactions between different proteins inside the spliceosome, or to initiate from its binding platforms isomerization or chaperoning, activities.
<StructureSection load='1mzw' size='340' side='right'caption='[[1mzw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mzw]] is a 2 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=1MZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzw OCA], [https://pdbe.org/1mzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzw RCSB], [https://www.ebi.ac.uk/pdbsum/1mzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPIH_HUMAN PPIH_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex. May act as a chaperone.<ref>PMID:9570313</ref> <ref>PMID:11823439</ref> <ref>PMID:12875835</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mzw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1mzw ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Cardiomyopathy, dilated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605906 605906]], Cardiomyopathy, dilated, with left ventricular noncompaction OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605906 605906]], Myopathy, myofibrillar, ZASP-related OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605906 605906]]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1MZW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MZW OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide., Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Luhrmann R, Ficner R, J Mol Biol. 2003 Aug 1;331(1):45-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12875835 12875835]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Ficner, R.]]
[[Category: Ficner R]]
[[Category: Horowitz, D.S.]]
[[Category: Horowitz DS]]
[[Category: Luehrmann, R.]]
[[Category: Luehrmann R]]
[[Category: Reidt, U.]]
[[Category: Reidt U]]
[[Category: Wahl, M.C.]]
[[Category: Wahl MC]]
[[Category: cyclophilin]]
[[Category: peptidyl-prolyl-cis/trans isomerase]]
[[Category: snrnp]]
[[Category: spliceosome]]
[[Category: u4/u6-60k protein]]
[[Category: wd protein]]
 
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Retrieved from "https://proteopedia.org/1mzw"