5mqf
From Proteopedia
(Difference between revisions)
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<SX load='5mqf' size='340' side='right' viewer='molstar' caption='[[5mqf]], [[Resolution|resolution]] 5.90Å' scene=''> | <SX load='5mqf' size='340' side='right' viewer='molstar' caption='[[5mqf]], [[Resolution|resolution]] 5.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5mqf]] is a | + | <table><tr><td colspan='2'>[[5mqf]] is a 11 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=5MQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MQF FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.9Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5mqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mqf OCA], [https://pdbe.org/5mqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mqf RCSB], [https://www.ebi.ac.uk/pdbsum/5mqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mqf 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=5mqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mqf OCA], [https://pdbe.org/5mqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mqf RCSB], [https://www.ebi.ac.uk/pdbsum/5mqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mqf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Disease == | ||
- | [https://www.uniprot.org/uniprot/PRP8_HUMAN PRP8_HUMAN] Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM:[https://omim.org/entry/600059 600059]. RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP13 inheritance is autosomal dominant.<ref>PMID:17317632</ref> <ref>PMID:11468273</ref> [:]<ref>PMID:11910553</ref> <ref>PMID:12714658</ref> | ||
== Function == | == Function == | ||
- | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/PPIE_HUMAN PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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*[[Helicase 3D structures|Helicase 3D structures]] | *[[Helicase 3D structures|Helicase 3D structures]] | ||
*[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]] | *[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]] | ||
- | *[[Sm-like protein|Sm-like protein]] | + | *[[Sm-like protein 3D structures|Sm-like protein 3D structures]] |
== References == | == References == | ||
<references/> | <references/> |
Current revision
Cryo-EM structure of a human spliceosome activated for step 2 of splicing (C* complex)
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