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Side-Chain Interact...
Side-Chain Interactions Form Late and Cooperatively in the Binding Reaction between Disordered Peptides and PDZ Domains
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- Haq, S Raza (author)
- Uppsala University
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- Chi, Celestine N. (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Uppsala University
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- Bach, Anders (author)
- University of Copenhagen
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- Dogan, Jakob (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Uppsala University
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- Engström, Åke (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Uppsala University
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- Hultqvist, Greta (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Uppsala University
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- Karlsson, O. Andreas (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Uppsala University
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- Lundström, Patrik (author)
- Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan
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- Montemiglio, Linda C (author)
- University of Roma La Sapienza
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- Stromgaard, Kristian (author)
- University of Copenhagen
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- Gianni, Stefano (author)
- University of Roma La Sapienza
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- Jemth, Per (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Uppsala University
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(creator_code:org_t)
- 2011-12-16
- 2012
- English.
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In: Journal of the American Chemical Society. - : American Chemical Society. - 0002-7863 .- 1520-5126. ; 134:1, s. 599-605
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Abstract
Subject headings
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- 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).
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Keyword
- TECHNOLOGY
- TEKNIKVETENSKAP
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Haq, S Raza
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Chi, Celestine N ...
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Bach, Anders
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Dogan, Jakob
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Engström, Åke
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Hultqvist, Greta
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show more...
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Karlsson, O. And ...
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Lundström, Patri ...
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Montemiglio, Lin ...
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Stromgaard, Kris ...
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Gianni, Stefano
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Jemth, Per
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
- Articles in the publication
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Journal of the A ...
- By the university
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Linköping University
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Uppsala University