1mzw

<table><tr><td colspan='2'>[[1mzw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qoi|1qoi]]</div></td></tr>

[[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> [[https://www.uniprot.org/uniprot/PRP4_HUMAN PRP4_HUMAN]] Involved in pre-mRNA splicing.

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== Publication Abstract from PubMed ==

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.

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:12875835<ref>PMID:12875835</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mzw" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Ficner, R]]

[[Category: Horowitz, D S]]

[[Category: Luehrmann, R]]

[[Category: Reidt, U]]

[[Category: Wahl, M C]]

[[Category: Wd protein]]