1qoi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:50, 13 December 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1qoi.gif|left|200px]]
 
-
<!--
+
==U4/U6 snRNP-specific cyclophilin SnuCyp-20==
-
The line below this paragraph, containing "STRUCTURE_1qoi", creates the "Structure Box" on the page.
+
<StructureSection load='1qoi' size='340' side='right'caption='[[1qoi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1qoi]] 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=1QOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOI FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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=1qoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoi OCA], [https://pdbe.org/1qoi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qoi RCSB], [https://www.ebi.ac.uk/pdbsum/1qoi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qoi ProSAT]</span></td></tr>
-
{{STRUCTURE_1qoi| PDB=1qoi | SCENE= }}
+
</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/qo/1qoi_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=1qoi ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The cyclophilin SnuCyp-20 is a specific component of the human U4/U6 small nuclear ribonucleoprotein particle involved in the nuclear splicing of pre-mRNA. It stably associates with the U4/U6-60kD and -90kD proteins, the human orthologues of the Saccharomyces cerevisiae Prp4 and Prp3 splicing factors. We have determined the crystal structure of SnuCyp-20 at 2.0-A resolution by molecular replacement. The structure of SnuCyp-20 closely resembles that of human cyclophilin A (hCypA). In particular, the catalytic centers of SnuCyp-20 and hCypA superimpose perfectly, which is reflected by the observed peptidyl-prolyl-cis/trans-isomerase activity of SnuCyp-20. The surface properties of both proteins, however, differ significantly. Apart from seven additional amino-terminal residues, the insertion of five amino acids in the loop alpha1-beta3 and of one amino acid in the loop alpha2-beta8 changes the conformations of both loops. The enlarged loop alpha1-beta3 is involved in the formation of a wide cleft with predominantly hydrophobic character. We propose that this enlarged loop is required for the interaction with the U4/U6-60kD protein.
-
'''U4/U6 SNRNP-SPECIFIC CYCLOPHILIN SNUCYP-20'''
+
Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin.,Reidt U, Reuter K, Achsel T, Ingelfinger D, Luhrmann R, Ficner R J Biol Chem. 2000 Mar 17;275(11):7439-42. PMID:10713041<ref>PMID:10713041</ref>
-
 
+
-
 
+
-
==Overview==
+
-
The cyclophilin SnuCyp-20 is a specific component of the human U4/U6 small nuclear ribonucleoprotein particle involved in the nuclear splicing of pre-mRNA. It stably associates with the U4/U6-60kD and -90kD proteins, the human orthologues of the Saccharomyces cerevisiae Prp4 and Prp3 splicing factors. We have determined the crystal structure of SnuCyp-20 at 2.0-A resolution by molecular replacement. The structure of SnuCyp-20 closely resembles that of human cyclophilin A (hCypA). In particular, the catalytic centers of SnuCyp-20 and hCypA superimpose perfectly, which is reflected by the observed peptidyl-prolyl-cis/trans-isomerase activity of SnuCyp-20. The surface properties of both proteins, however, differ significantly. Apart from seven additional amino-terminal residues, the insertion of five amino acids in the loop alpha1-beta3 and of one amino acid in the loop alpha2-beta8 changes the conformations of both loops. The enlarged loop alpha1-beta3 is involved in the formation of a wide cleft with predominantly hydrophobic character. We propose that this enlarged loop is required for the interaction with the U4/U6-60kD protein.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1QOI is a [[Single protein]] structure of sequence 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=1QOI OCA].
+
</div>
 +
<div class="pdbe-citations 1qoi" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin., Reidt U, Reuter K, Achsel T, Ingelfinger D, Luhrmann R, Ficner R, J Biol Chem. 2000 Mar 17;275(11):7439-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10713041 10713041]
+
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Achsel, T.]]
+
[[Category: Achsel T]]
-
[[Category: Ficner, R.]]
+
[[Category: Ficner R]]
-
[[Category: Ingelfinger, D.]]
+
[[Category: Ingelfinger D]]
-
[[Category: Luehrmann, R.]]
+
[[Category: Luehrmann R]]
-
[[Category: Reidt, U.]]
+
[[Category: Reidt U]]
-
[[Category: Reuter, K.]]
+
[[Category: Reuter K]]
-
[[Category: Cyclophilin]]
+
-
[[Category: Snrnp]]
+
-
[[Category: Snucyp-20]]
+
-
[[Category: Spliceosomal]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:31:07 2008''
+

Current revision

U4/U6 snRNP-specific cyclophilin SnuCyp-20

PDB ID 1qoi

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qoi"
Personal tools