Structural highlights
Function
PLRG1_HUMAN Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.
Publication Abstract from PubMed
PLRG1 is a evolutionarily conserved protein in spliceosome and plays an important role in maintaining the integral part of the splicoeosme and its proper splicing. Here we solved the high resolution crystal structure of the WD40 domain of human PLRG1 by crystallography and compared our crystal structure with the cryo-EM structure of PLRG1 bound with other splicing factors. We found that two loops of the WD40 domain become resolved upon binding to the proteins within the spliceosome. Thus our work characterize the dynamic property of PLRG1 during the spliceosome assembly by presenting its apo structure.
Crystal structure of the WD40 domain of human PLRG1.,Wang X, Li Y, Dai H, Xu C Biochem Biophys Res Commun. 2021 Jan 1;534:474-477. doi:, 10.1016/j.bbrc.2020.11.057. Epub 2020 Nov 22. PMID:33239170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, Li Y, Dai H, Xu C. Crystal structure of the WD40 domain of human PLRG1. Biochem Biophys Res Commun. 2021 Jan 1;534:474-477. doi:, 10.1016/j.bbrc.2020.11.057. Epub 2020 Nov 22. PMID:33239170 doi:http://dx.doi.org/10.1016/j.bbrc.2020.11.057
