4bf8: Difference between revisions
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{{STRUCTURE_4bf8| PDB=4bf8 | SCENE= }} | {{STRUCTURE_4bf8| PDB=4bf8 | SCENE= }} | ||
===Fpr4 PPI domain=== | ===Fpr4 PPI domain=== | ||
{{ABSTRACT_PUBMED_23888048}} | |||
==Function== | ==Function== | ||
| Line 7: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
[[4bf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BF8 OCA]. | [[4bf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BF8 OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:023888048</ref><references group="xtra"/><references/> | |||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
Revision as of 18:59, 7 August 2013
Fpr4 PPI domain
Template:ABSTRACT PUBMED 23888048
Function
[FKBP4_YEAST] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
About this Structure
4bf8 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.
Reference
- Monneau YR, Soufari H, Nelson CJ, Mackereth CD. Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 towards histone H3 proline isomerization. J Biol Chem. 2013 Jul 25. PMID:23888048 doi:10.1074/jbc.M113.479964
