2p8r

<StructureSection load='2p8r' size='340' side='right' caption='[[2p8r]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[2p8r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P8R FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prp-8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=2p8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p8r OCA], [http://pdbe.org/2p8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p8r RCSB], [http://www.ebi.ac.uk/pdbsum/2p8r PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PRP8_CAEEL PRP8_CAEEL]] Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p8/2p8r_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Prp8 is a critical pre-mRNA splicing factor. Prp8 is proposed to help form and stabilize the spliceosome catalytic core and to be an important regulator of spliceosome activation. Mutations in human Prp8 (hPrp8) cause a severe form of the genetic disorder retinitis pigmentosa, RP13. Understanding the molecular mechanism of Prp8's function in pre-mRNA splicing and RP13 has been hindered by its large size (over 2000 amino acids) and remarkably low-sequence similarity with other proteins. Here we present the crystal structure of the C-terminal domain (the last 273 residues) of Caenorhabditis elegans Prp8 (cPrp8). The core of the C-terminal domain is an alpha/beta structure that forms the MPN (Mpr1, Pad1 N-terminal) fold but without Zn(2+) coordination. We propose that the C-terminal domain is a protein interaction domain instead of a Zn(2+)-dependent metalloenzyme as proposed for some MPN proteins. Mapping of RP13 mutants on the Prp8 structure suggests that these residues constitute a binding surface between Prp8 and other partner(s), and the disruption of this interaction provides a plausible molecular mechanism for RP13.

Crystal structure of the C-terminal domain of splicing factor Prp8 carrying retinitis pigmentosa mutants.,Zhang L, Shen J, Guarnieri MT, Heroux A, Yang K, Zhao R Protein Sci. 2007 Jun;16(6):1024-31. Epub 2007 May 1. PMID:17473007<ref>PMID:17473007</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 2p8r" style="background-color:#fffaf0;"></div>

*[[Pre-mRNA-splicing factor|Pre-mRNA-splicing factor]]

[[Category: Caeel]]

[[Category: Guarnieri, M T]]

[[Category: Heroux, A]]

[[Category: Shen, J]]

[[Category: Yang, K]]

[[Category: Zhang, L]]

[[Category: Zhao, R]]

[[Category: Translation]]