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Affinity and specificity of motif-based protein-protein interactions
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. Uppsala universitet.ORCID iD: 0000-0002-7081-3846
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. Uppsala universitet.ORCID iD: 0000-0003-1516-7228
2019 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 54, p. 26-33Article, review/survey (Refereed) Published
Abstract [en]

It is becoming increasingly clear that eukaryotic cell physiology is largely controlled by protein protein interactions involving disordered protein regions, which usually interact with globular domains in a coupled binding and folding reaction. Several protein recognition domains are part of large families where members can interact with similar peptide ligands. Because of this, much research has been devoted to understanding how specificity can be achieved. A combination of interface complementarity, interactions outside of the core binding site, avidity from multidomain architecture and spatial and temporal regulation of expression resolves the conundrum. Here, we review recent advances in molecular aspects of affinity and specificity in such protein-protein interactions.

Place, publisher, year, edition, pages
Current Biology , 2019. Vol. 54, p. 26-33
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:uu:diva-362357DOI: 10.1016/j.sbi.2018.09.009ISI: 000473554100005PubMedID: 30368054OAI: oai:DiVA.org:uu-362357DiVA, id: diva2:1253121
Funder
Swedish Foundation for Strategic Research , SB16-0039Swedish Research Council, 2016-04965Swedish Research Council, 2016-04134Available from: 2018-10-03 Created: 2018-10-03 Last updated: 2019-08-08Bibliographically approved

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Ivarsson, YlvaJemth, Per

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