Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Side-Chain Interactions Form Late and Cooperatively in the Binding Reaction between Disordered Peptides and PDZ Domains
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Show others and affiliations
2012 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 134, no 1, p. 599-605Article in journal (Refereed) Published
Abstract [en]

Intrinsically disordered proteins are very common and mediate numerous protein-protein and protein-DNA interactions. While it is clear that these interactions are instrumental for the life of the mammalian cell, there is a paucity of data regarding their molecular binding mechanisms. Here we have used short peptides as a model system for intrinsically disordered proteins. Linear free energy relationships based on rate and equilibrium constants for the binding of these peptides to ordered target proteins, PDZ domains, demonstrate that native side-chain interactions form mainly after the rate-limiting barrier for binding and in a cooperative fashion. This finding suggests that these disordered peptides first form a weak encounter complex with non-native interactions. The data do not support the recent notion that the affinities of intrinsically disordered proteins toward their targets are generally governed by their association rate constants. Instead, we observed the opposite for peptide-PDZ interactions, namely, that changes in K-d correlate with changes in k(off).

Place, publisher, year, edition, pages
2012. Vol. 134, no 1, p. 599-605
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-172158DOI: 10.1021/ja209341wISI: 000301084200096OAI: oai:DiVA.org:uu-172158DiVA, id: diva2:513743
Available from: 2012-04-03 Created: 2012-04-02 Last updated: 2017-12-07Bibliographically approved

Open Access in DiVA

fulltext(1579 kB)212 downloads
File information
File name FULLTEXT01.pdfFile size 1579 kBChecksum SHA-512
51e211c22e4e5db05355e81759176abae4def6fd0f96503cb0db6f9f3cb5e03f13df692475b02e8bcb8fa7e12f4e76636f4c3e267f20a0743e8fe4e893e405c2
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Search in DiVA

By author/editor
Chi, Celestine N.Dogan, JakobEngström, ÅkeHultqvist, GretaKarlsson, O. AndreasJemth, Per
By organisation
Department of Medical Biochemistry and Microbiology
In the same journal
Journal of the American Chemical Society
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar
Total: 212 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 792 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf