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='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.<ref>pmid:11274149.</ref> 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.<ref>pmid:11274149.</ref> 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.

==WD40 Domain==

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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='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.<ref>pmid:11274149.</ref> 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.<ref>pmid:11274149.</ref> 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.
 ==WD40 Domain==