1mzw: Difference between revisions
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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'''Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide'''<br /> | '''Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide'''<br /> | ||
==Overview== | ==Overview== | ||
The spliceosomal cyclophilin H is a specific component of the human U4/U6 | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
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:// | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
[[Category: Horowitz, D | [[Category: Horowitz, D S.]] | ||
[[Category: Luehrmann, R.]] | [[Category: Luehrmann, R.]] | ||
[[Category: Reidt, U.]] | [[Category: Reidt, U.]] | ||
[[Category: Wahl, M | [[Category: Wahl, M C.]] | ||
[[Category: cyclophilin]] | [[Category: cyclophilin]] | ||
[[Category: peptidyl-prolyl-cis/trans isomerase]] | [[Category: peptidyl-prolyl-cis/trans isomerase]] | ||
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[[Category: wd protein]] | [[Category: wd protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:47 2008'' | ||
Revision as of 15:00, 21 February 2008
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Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Cardiomyopathy, dilated OMIM:[605906], Cardiomyopathy, dilated, with left ventricular noncompaction OMIM:[605906], Myopathy, myofibrillar, ZASP-related OMIM:[605906]
About this StructureAbout this Structure
1MZW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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