期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 54, 期 -, 页码 26-33出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2018.09.009
关键词
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资金
- Swedish foundation for strategic research [SB16-0039]
- Swedish research council [2016-04965, 2016-04134]
- Vinnova [2016-04134] Funding Source: Vinnova
- Swedish Foundation for Strategic Research (SSF) [SB16-0039] Funding Source: Swedish Foundation for Strategic Research (SSF)
- Swedish Research Council [2016-04965, 2016-04134] Funding Source: Swedish Research Council
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.
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