3lru
From Proteopedia
hPRP8 Non-Native Subdomain
Structural highlights
Disease[PRP8_HUMAN] Defects in PRPF8 are the cause of retinitis pigmentosa type 13 (RP13) [MIM: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.[1] [2] [:][3] [4] Function[PRP8_HUMAN] Central component of the spliceosome, which may play a role in aligning the pre-mRNA 5'- and 3'-exons for ligation. Interacts with U5 snRNA, and with pre-mRNA 5'-splice sites in B spliceosomes and 3'-splice sites in C spliceosomes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein folding involves the formation of secondary structural elements from the primary sequence and their association with tertiary assemblies. The relation of this primary sequence to a specific folded protein structure remains a central question in structural biology. An increasing body of evidence suggests that variations in homologous sequence ranging from point mutations to substantial insertions or deletions can yield stable proteins with markedly different folds. Here we report the structural characterization of domain IV (D4) and DeltaD4 (polypeptides with 222 and 160 amino acids, respectively) that differ by virtue of an N-terminal deletion of 62 amino acids (28% of the overall D4 sequence). The high-resolution crystal structures of the monomeric D4 and the dimeric DeltaD4 reveal substantially different folds despite an overall conservation of secondary structure. These structures show that the formation of tertiary structures, even in extended polypeptide sequences, can be highly context dependent, and they serve as a model for structural plasticity in protein isoforms. Context-dependent remodeling of structure in two large protein fragments.,Schellenberg MJ, Ritchie DB, Wu T, Markin CJ, Spyracopoulos L, MacMillan AM J Mol Biol. 2010 Oct 1;402(4):720-30. Epub 2010 Aug 14. PMID:20713060[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Human | MacMillan, A M | Ritchie, D B | Schellenberg, M J | Alternate folding of protein | Disease mutation | Mrna processing | Mrna splicing | Nucleus | Phosphoprotein | Retinitis pigmentosa | Ribonucleoprotein | Rna binding protein | Rna-binding | Sensory transduction | Spliceosome | Vision
