Peptidyl-prolyl cis-trans isomerase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Peptidyl-prolyl cis-trans isomerase''' (PPIase) interconverts cis and trans isomers of proline. PPIase functions as a protein folding chaperone. The 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. The PPIase macrophage infectivity potentiator | + | '''Peptidyl-prolyl cis-trans isomerase''' (PPIase) interconverts cis and trans isomers of proline. PPIase functions as a protein folding chaperone. The '''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. The '''PPIase Mip''' (macrophage infectivity potentiator) is required for optimal infection of macrophages by some parasites. The '''PPIase SlyD''' acts as a chaperone and speeds up protein folding. |
For various types of PPIase see:<br /> | For various types of PPIase see:<br /> | ||
Revision as of 06:57, 10 May 2015
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3D Structures of peptidyl-prolyl cis-trans isomerase
Updated on 10-May-2015
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
