期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 22, 期 4, 页码 432-441出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2012.03.002
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资金
- BBSRC
- EPSRC of the UK [BB/G008833/1, EP/J01430/1]
- Biotechnology and Biological Sciences Research Council [BB/G008833/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J001430/1] Funding Source: researchfish
- BBSRC [BB/G008833/1] Funding Source: UKRI
- EPSRC [EP/J001430/1] Funding Source: UKRI
alpha-Helical coiled coils are ubiquitous protein-protein-interaction domains. They share a relatively straightforward sequence repeat, which directs the folding and assembly of amphipathic helices. The helices can combine in a number of oligonnerisation states and topologies to direct a wide variety of protein assemblies. Although in nature parallel dimers, trimers and tetramers dominate, the potential to form larger oligomers and more-complex assemblies has long been recognised. In particular, complexes above pentamer are interesting because they are barrel-like, having central channels or pores with well-defined dimensions and chemistry. Recent empirical and rational design experiments are beginning to chart this potential new territory in coiled-coil space, leading to intriguing new structures, and possibilities for functionalisation and applications.
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