4lg8
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/PRP19_HUMAN PRP19_HUMAN]] Plays a role in DNA double-strand break (DSB) repair. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.<ref>PMID:11082287</ref> <ref>PMID:12960389</ref> <ref>PMID:16332694</ref> <ref>PMID:15660529</ref> <ref>PMID:16223718</ref> <ref>PMID:16388800</ref> | [[http://www.uniprot.org/uniprot/PRP19_HUMAN PRP19_HUMAN]] Plays a role in DNA double-strand break (DSB) repair. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.<ref>PMID:11082287</ref> <ref>PMID:12960389</ref> <ref>PMID:16332694</ref> <ref>PMID:15660529</ref> <ref>PMID:16223718</ref> <ref>PMID:16388800</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human Pre-mRNA Processing factor 19 (hPRPF19) is an important component in human spliceosome machinery. hPRPF19 contains a WD40 repeats domain at its C-terminus, which is also conserved in yeast. Here we determined the crystal structure of the C-terminal WD40 repeat domain of hPRPF19 by X-ray crystallography. Our structural analysis revealed some significantly different structure features between the human and yeast Prp19 WD40 repeat domain. However, there are also conserved clusters of residues at the bottom surface of the fourth and the fifth WD40 repeats, which provides the important implication for the conserved Prp19 proteins in both human and yeast. | ||
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| + | Crystal structure of the WD40 domain of human PRPF19.,Zhang Y, Li Y, Liang X, Zhu Z, Sun H, He H, Min J, Liao S, Liu Y Biochem Biophys Res Commun. 2017 Nov 25;493(3):1250-1253. doi:, 10.1016/j.bbrc.2017.09.145. Epub 2017 Sep 28. PMID:28962858<ref>PMID:28962858</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4lg8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:54, 3 January 2018
Crystal structure of PRPF19 WD40 repeats
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Categories: Human | Arrowsmith, C H | Bountra, C | Dobrovetsky, E | Edwards, A M | He, H | Min, J | Structural genomic | Seitova, A | Tempel, W | Xu, C | Dna binding protein | Sgc | Wd40 repeat
