Prp19: Difference between revisions
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U-Box proteins are a class of ubiquitin ligases whose structures are generally stabilized by hydrogen bond and or salt bridges. In mammals, these proteins have been found to associate and interact with molecular chaperons such as HSP90 and HSP70, providing evidence that they may be involved in the degradation of mis-folded proteins.<ref>http://smart.embl-heidelberg.de/smart/do_annotation.pl?ACC=SM00504</ref> PRP19's U-Box domain is located at the beginning of its amino acid sequence and is comprised of 61 residues. The U-Box domain's structure was first solved by NMR in 2003<Ref>pmid:12627222</ref> and by X-ray crystallography in 2006<ref name="something"/> | U-Box proteins are a class of ubiquitin ligases whose structures are generally stabilized by hydrogen bond and or salt bridges. In mammals, these proteins have been found to associate and interact with molecular chaperons such as HSP90 and HSP70, providing evidence that they may be involved in the degradation of mis-folded proteins.<ref>http://smart.embl-heidelberg.de/smart/do_annotation.pl?ACC=SM00504</ref> PRP19's U-Box domain is located at the beginning of its amino acid sequence and is comprised of 61 residues. The U-Box domain's structure was first solved by NMR in 2003<Ref>pmid:12627222</ref> and by X-ray crystallography in 2006<ref name="something"/> | ||
==WD40 Domain== | |||
=Role in Splicing= | =Role in Splicing= | ||
