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Mapping the transit...
Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins
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- Karlsson, Elin (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Paissoni, Cristina (författare)
- Univ Milan, Dipartimento Biosci, Milan, Italy.
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- Erkelens, Amanda M. (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Leiden Univ, Dept Chem, Leiden, Netherlands.
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- Tehranizadeh, Zeinab A. (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Mashhad Univ Med Sci, Sch Pharm, Dept Med Chem, Mashhad, Razavi Khorasan, Iran.
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- Sorgenfrei, Frieda A. (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Karl Franzens Univ Graz, Inst Organ & Bioorgan Chem, Dept Chem, Heinrichstr, Graz, Austria.
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- Andersson, Eva (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Ye, Weihua (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Camilloni, Carlo (författare)
- Univ Milan, Dipartimento Biosci, Milan, Italy.
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- Jemth, Per (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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(creator_code:org_t)
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2020
- 2020
- Engelska.
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Ingår i: Journal of Biological Chemistry. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258 .- 1083-351X. ; 295:51, s. 17698-17712
- Relaterad länk:
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https://doi.org/10.1...
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https://uu.diva-port... (primary) (Raw object)
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Intrinsically disordered protein domains often have multiple binding partners. It is plausible that the strength of pairing with specific partners evolves from an initial low affinity to a higher affinity. However, little is known about the molecular changes in the binding mechanism that would facilitate such a transition. We previously showed that the interaction between two intrinsically disordered domains, NCBD and CID, likely emerged in an ancestral deuterostome organism as a low-affinity interaction that subsequently evolved into a higher-affinity interaction before the radiation of modern vertebrate groups. Here we map native contacts in the transition states of the low-affinity ancestral and high-affinity human NCBD/CID interactions. We show that the coupled binding and folding mechanism is overall similar but with a higher degree of native hydrophobic contact formation in the transition state of the ancestral complex and more heterogeneous transient interactions, including electrostatic pairings, and an increased disorder for the human complex. Adaptation to new binding partners may be facilitated by this ability to exploit multiple alternative transient interactions while retaining the overall binding and folding pathway.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- intrinsically disordered proteins
- phi value analysis
- transition state
- protein evolution
- coupled binding and folding
- protein folding
- pre-steady-state kinetics
- protein complex
- IDP
- protein binding
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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