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1mzw

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Revision as of 06:57, 25 August 2021

Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide

Structural highlights

1mzw is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1qoi
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] [PRP4_HUMAN] Involved in pre-mRNA splicing.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Teigelkamp S, Achsel T, Mundt C, Gothel SF, Cronshagen U, Lane WS, Marahiel M, Luhrmann R. The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins. RNA. 1998 Feb;4(2):127-41. PMID:9570313
↑ Horowitz DS, Lee EJ, Mabon SA, Misteli T. A cyclophilin functions in pre-mRNA splicing. EMBO J. 2002 Feb 1;21(3):470-80. PMID:11823439
↑ Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Luhrmann R, Ficner R. Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol. 2003 Aug 1;331(1):45-56. PMID:12875835
↑ Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Luhrmann R, Ficner R. Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol. 2003 Aug 1;331(1):45-56. PMID:12875835

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mzw"

@@ Line 3: / Line 3: @@
 <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MZW FirstGlance]. <br>
+<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">[[1qoi|1qoi]]</td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzw OCA], [http://pdbe.org/1mzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mzw RCSB], [http://www.ebi.ac.uk/pdbsum/1mzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzw ProSAT]</span></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 ==
-[[http://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>  [[http://www.uniprot.org/uniprot/PRP4_HUMAN PRP4_HUMAN]] Involved in pre-mRNA splicing.
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mzw

From Proteopedia

Revision as of 06:57, 25 August 2021

Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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