Peptidyl-prolyl cis-trans isomerase
From Proteopedia
(Difference between revisions)
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**[[2m08]] – PPIase – ''Nitrosopumilus maritimus'' - NMR<BR /> | **[[2m08]] – PPIase – ''Nitrosopumilus maritimus'' - NMR<BR /> | ||
| - | *PPIase Pin1 | + | *PPIase Pin1; Domains – WW 1-39; PPIase 51-163 |
**[[1pin]] – hPin1 – human<BR /> | **[[1pin]] – hPin1 – human<BR /> | ||
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**[[1zcn]], [[2zqs]], [[2zqt]], [[2zqu]], [[2zqv]], [[2zr4]], [[2zr5]], [[2zr6]] – hPin1 (mutant)<BR /> | **[[1zcn]], [[2zqs]], [[2zqt]], [[2zqu]], [[2zqv]], [[2zr4]], [[2zr5]], [[2zr6]] – hPin1 (mutant)<BR /> | ||
**[[1i6c]], [[2kcf]], [[2kbu]], [[1eq3]], [[2m8i]], [[2m8j]] – hPin1 WW domain - NMR<BR /> | **[[1i6c]], [[2kcf]], [[2kbu]], [[1eq3]], [[2m8i]], [[2m8j]] – hPin1 WW domain - NMR<BR /> | ||
| - | **[[2f21]], [[1fjd]], [[2m9e]], [[2m9f]], [[2m9i]], [[2m9j]] – hPin1 WW domain (mutant)<BR /> | + | **[[2f21]], [[1fjd]], [[2m9e]], [[2m9f]], [[2m9i]], [[2m9j]], [[5vti]], [[5vtj]], [[5vtk]] – hPin1 WW domain (mutant)<BR /> |
**[[3ik8]] – hPin1 PPIase domain (mutant)<BR /> | **[[3ik8]] – hPin1 PPIase domain (mutant)<BR /> | ||
| - | **[[2rud]] – hPin1 PPIase domain (mutant) - NMR<BR /> | + | **[[2rud]], [[5gph]] – hPin1 PPIase domain (mutant) - NMR<BR /> |
**[[1nmw]], [[2ruc]] – hPin1 PPIase domain - NMR<BR /> | **[[1nmw]], [[2ruc]] – hPin1 PPIase domain - NMR<BR /> | ||
**[[1j6y]] – Pin1 – ''Arabidopsis thaliana'' - NMR<BR /> | **[[1j6y]] – Pin1 – ''Arabidopsis thaliana'' - NMR<BR /> | ||
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*PPIase Pin1 complexes | *PPIase Pin1 complexes | ||
| - | **[[1f8a]] – hPin1 + phosphoserine containing peptide<BR /> | + | **[[1f8a]], [[5uy9]] – hPin1 + phosphoserine containing peptide<BR /> |
**[[1i8g]], [[1i8h]] – hPin1 WW domain + phosphothreoniine containing peptide - NMR<BR /> | **[[1i8g]], [[1i8h]] – hPin1 WW domain + phosphothreoniine containing peptide - NMR<BR /> | ||
**[[2lb3]] – hPin1 WW domain + MAD homolog peptide - NMR<BR /> | **[[2lb3]] – hPin1 WW domain + MAD homolog peptide - NMR<BR /> | ||
Revision as of 09:47, 16 August 2018
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3D Structures of peptidyl-prolyl cis-trans isomerase
Updated on 16-August-2018
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
- ↑ Fischer G, Bang H, Ludwig B, Mann K, Hacker J. Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity. Mol Microbiol. 1992 May;6(10):1375-83. PMID:1379319
- ↑ 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
- ↑ McClements L, Annett S, Yakkundi A, Robson T. The Role of Peptidyl Prolyl Isomerases in Aging and Vascular Diseases. Curr Mol Pharmacol. 2015;9(2):165-79. PMID:25986561
- ↑ Westerman ST. Tasting instilled otologic drops is not a reliable test of eustachian tube function. Arch Otolaryngol Head Neck Surg. 2000 Aug;126(8):1042. PMID:10922246
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