Prp19: Difference between revisions

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[[Image:2bay_small.jpg]] This is a CPK coloured representation of the U Box Domain of PRP19. The secondary structure can be seen <scene name=2bay>here</scene>

[[Image:2bay_small.jpg]] This is a CPK coloured representation of the U Box Domain of PRP19. The secondary structure can be seen <scene name='prp19/2bay/3'>here</scene>

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"/> The protein was purified from yeast (''S. cerevisiae'') and the resulting crystal structure was solved via xray diffraction at a resolution of 1.5 Angstroms and revealed that the U-Box fragment consisted of six chains.

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Revision as of 03:44, 1 April 2011 view source Aaron Smith (talk \| contribs) 215 edits →U-Box Domain ← Older edit		Revision as of 03:46, 1 April 2011 view source Aaron Smith (talk \| contribs) 215 edits →U-Box Domain Newer edit →
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	[[Image:2bay_small.jpg]] This is a CPK coloured representation of the U Box Domain of PRP19. The secondary structure can be seen <scene name=2bay>here</scene>		[[Image:2bay_small.jpg]] This is a CPK coloured representation of the U Box Domain of PRP19. The secondary structure can be seen <scene name='prp19/2bay/3'>here</scene>

	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"/> The protein was purified from yeast (''S. cerevisiae'') and the resulting crystal structure was solved via xray diffraction at a resolution of 1.5 Angstroms and revealed that the U-Box fragment consisted of six chains.		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"/> The protein was purified from yeast (''S. cerevisiae'') and the resulting crystal structure was solved via xray diffraction at a resolution of 1.5 Angstroms and revealed that the U-Box fragment consisted of six chains.