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Addressing the role of the alpha-helical extension in the folding of the third PDZ domain from PSD-95
Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy..
Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy..
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, Ist Biol & Patol Mol, CNR, I-00185 Rome, Italy..
2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, article id 12593Article in journal (Refereed) Published
Abstract [en]

PDZ domains are one of the most important protein-protein interaction domains in human. While presenting a conserved three dimensional structure, a substantial number of PDZ domains display structural extensions suggested to be involved in their folding and binding mechanisms. The C-terminal a-helix extension (alpha 3) of the third PDZ domain from PSD-95 (PDZ3) has been reported to have a role in function of the domain as well as in the stabilization of the native fold. Here we report an evaluation of the effect of the truncation of this additional helix on the folding and unfolding kinetics of PDZ3. Fluorescent variants of full length and truncated PDZ3 were produced and stopped-flow fluorescence measurements were made under different experimental conditions (pH, ionic strength and temperature) to investigate the folding kinetics of the respective variant. The results show that folding of PDZ3 is robust and that the mechanism is only marginally affected by the truncation, which contributes to a destabilization of the native state, but otherwise do not change the overall observed kinetics. Furthermore, the increase in the unfolding rate constants, but not the folding rate constant upon deletion of alpha 3 suggests that the a-helical extension is largely unstructured in the folding transition state.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP , 2017. Vol. 7, article id 12593
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-337114DOI: 10.1038/s41598-017-12827-0ISI: 000412138800029PubMedID: 28974728OAI: oai:DiVA.org:uu-337114DiVA, id: diva2:1168565
Funder
EU, Horizon 2020, 675341Available from: 2017-12-21 Created: 2017-12-21 Last updated: 2017-12-21Bibliographically approved

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