4bf8

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{{STRUCTURE_4bf8| PDB=4bf8 | SCENE= }}
{{STRUCTURE_4bf8| PDB=4bf8 | SCENE= }}
===Fpr4 PPI domain===
===Fpr4 PPI domain===
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{{ABSTRACT_PUBMED_23888048}}
==Function==
==Function==
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==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].
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==Reference==
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<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

Template:STRUCTURE 4bf8

Contents

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

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