Peptidyl-prolyl cis-trans isomerase
From Proteopedia
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'''Peptidyl-prolyl cis-trans isomerase''' (PPIase) interconverts cis and trans isomers of proline. PPIase functions as a protein folding chaperone.<br /> | '''Peptidyl-prolyl cis-trans isomerase''' (PPIase) interconverts cis and trans isomers of proline. PPIase functions as a protein folding chaperone.<br /> | ||
| - | * '''PPIase Pin1''' isomerizes phospho-serine/threonine proline motifs. The deregulation of Pin1 may be involved in cancer and Alzheimer Disease. Pin1 consists of 2 domains: the WW domain recognizes the pSer/pThr Pro motif and the PPIase domain contains the catalytic site.<br /> | + | * '''PPIase Pin1''' isomerizes phospho-serine/threonine proline motifs<ref>PMID:24173213</ref>. The deregulation of Pin1 may be involved in cancer and Alzheimer Disease. Pin1 consists of 2 domains: the WW domain recognizes the pSer/pThr Pro motif and the PPIase domain contains the catalytic site.<br /> |
* '''PPIase Mip''' (macrophage infectivity potentiator) is required for optimal infection of macrophages by some parasites.<br /> | * '''PPIase Mip''' (macrophage infectivity potentiator) is required for optimal infection of macrophages by some parasites.<br /> | ||
| - | * '''PPIase SlyD''' acts as a chaperone and speeds up protein folding. | + | * '''PPIase SlyD''' acts as a chaperone and speeds up protein folding.<br /> |
| + | * '''PPIase SlpA''' is a 2-domain protein containing an FK506-binding domain and a PPIase domain and a small insert-in-flap domain which acts as a chaperone<ref>PMID:22735173</ref>.<br /> | ||
For various types of PPIase see:<br /> | For various types of PPIase see:<br /> | ||
Revision as of 09:21, 20 June 2016
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3D Structures of peptidyl-prolyl cis-trans isomerase
Updated on 20-June-2016
References
- ↑ Guito J, Gavina A, Palmeri D, Lukac DM. The cellular peptidyl-prolyl cis/trans isomerase Pin1 regulates reactivation of Kaposi's sarcoma-associated herpesvirus from latency. J Virol. 2014 Jan;88(1):547-58. doi: 10.1128/JVI.02877-13. Epub 2013 Oct 30. PMID:24173213 doi:http://dx.doi.org/10.1128/JVI.02877-13
- ↑ Quistgaard EM, Nordlund P, Low C. High-resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA. FASEB J. 2012 Jun 26. PMID:22735173 doi:10.1096/fj.12-208397
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