Peptide binding induces large scale changes in inter-domain mobility in human Pin1 - PubMed (original) (raw)
. 2003 Jul 11;278(28):26174-82.
doi: 10.1074/jbc.M300796200. Epub 2003 Apr 9.
Affiliations
- PMID: 12686540
- DOI: 10.1074/jbc.M300796200
Free article
Peptide binding induces large scale changes in inter-domain mobility in human Pin1
Doris M Jacobs et al. J Biol Chem. 2003.
Free article
Abstract
Pin1 is a peptidyl-prolyl cis/trans isomerase (PPIase) essential for cell cycle regulation. Pin1-catalyzed peptidyl-prolyl isomerization provides a key conformational switch to activate phosphorylation sites with the common phospho-Ser/Thr-Pro sequence motif. This motif is ubiquitously exploited in cellular response to a variety of signals. Pin1 is able to bind phospho-Ser/Thr-Pro-containing sequences at two different sites that compete for the same substrate. One binding site is located within the N-terminal WW domain, which is essential for protein targeting and localization. The other binding site is located in the C-terminal catalytic domain, which is structural homologous to the FK506-binding protein (FKBP) class of PPIases. A flexible linker of 12 residues connects the WW and catalytic domain. To characterize the structure and dynamics of full-length Pin1 in solution, high resolution NMR methods have been used to map the nature of interactions between the two domains of Pin1. In addition, the influence of target peptides on domain interactions has been investigated. The studies reveal a dynamic picture of the domain interactions. 15N spin relaxation data, differential chemical shift mapping, and residual dipolar coupling data indicate that Pin1 can either behave as two independent domains connected by the flexible linker or as a single intact domain with some amount of hinge bending motion depending on the sequence of the bound peptide. The functional importance of the modulation of relative domain flexibility in light of the multitude of interaction partners of Pin1 is discussed.
Similar articles
- On the benefit of bivalency in peptide ligand/pin1 interactions.
Daum S, Lücke C, Wildemann D, Schiene-Fischer C. Daum S, et al. J Mol Biol. 2007 Nov 16;374(1):147-61. doi: 10.1016/j.jmb.2007.09.019. Epub 2007 Sep 14. J Mol Biol. 2007. PMID: 17931657 - The Peptidyl-Prolyl cis-trans isomerase, Pin1, associates with Protein Kinase C θ via a critical Phospho-Thr-Pro motif in the V3 regulatory domain.
Anto NP, Muraleedharan A, Nath PR, Sun Z, Keasar C, Livneh E, Braiman A, Altman A, Kong KF, Isakov N. Anto NP, et al. Front Immunol. 2023 Mar 8;14:1126464. doi: 10.3389/fimmu.2023.1126464. eCollection 2023. Front Immunol. 2023. PMID: 36969236 Free PMC article. - Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.
Landrieu I, Wieruszeski JM, Wintjens R, Inzé D, Lippens G. Landrieu I, et al. J Mol Biol. 2002 Jul 5;320(2):321-32. doi: 10.1016/S0022-2836(02)00429-1. J Mol Biol. 2002. PMID: 12079389 - Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism.
Zhou XZ, Lu PJ, Wulf G, Lu KP. Zhou XZ, et al. Cell Mol Life Sci. 1999 Nov 30;56(9-10):788-806. doi: 10.1007/s000180050026. Cell Mol Life Sci. 1999. PMID: 11212339 Free PMC article. Review. - Exploring the molecular function of PIN1 by nuclear magnetic resonance.
Landrieu I, Smet C, Wieruszeski JM, Sambo AV, Wintjens R, Buée L, Lippens G. Landrieu I, et al. Curr Protein Pept Sci. 2006 Jun;7(3):179-94. doi: 10.2174/138920306777452303. Curr Protein Pept Sci. 2006. PMID: 16787258 Review.
Cited by
- Ligand-specific conformational change drives interdomain allostery in Pin1.
Born A, Soetbeer J, Henen MA, Breitgoff F, Polyhach Y, Jeschke G, Vögeli B. Born A, et al. Nat Commun. 2022 Aug 4;13(1):4546. doi: 10.1038/s41467-022-32340-x. Nat Commun. 2022. PMID: 35927276 Free PMC article. - SxIP binding disrupts the constitutive homodimer interface of EB1 and stabilizes EB1 monomer.
Ayyappan S, Dharan PS, Krishnan A, Marira RR, Lambert M, Manna TK, Vijayan V. Ayyappan S, et al. Biophys J. 2021 May 18;120(10):2019-2029. doi: 10.1016/j.bpj.2021.03.004. Epub 2021 Mar 16. Biophys J. 2021. PMID: 33737159 Free PMC article. - Regulation of eukaryotic protein kinases by Pin1, a peptidyl-prolyl isomerase.
Chen XR, Igumenova TI. Chen XR, et al. Adv Biol Regul. 2023 Jan;87:100938. doi: 10.1016/j.jbior.2022.100938. Epub 2022 Nov 30. Adv Biol Regul. 2023. PMID: 36496344 Free PMC article. - Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1.
Lee YM, Liou YC. Lee YM, et al. Front Oncol. 2018 Oct 25;8:469. doi: 10.3389/fonc.2018.00469. eCollection 2018. Front Oncol. 2018. PMID: 30460195 Free PMC article. Review. - On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins.
Born A, Henen MA, Nichols PJ, Vögeli B. Born A, et al. Magn Reson Lett. 2022 May;2(2):61-68. doi: 10.1016/j.mrl.2021.10.003. Epub 2021 Nov 2. Magn Reson Lett. 2022. PMID: 35734611 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous