کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2184270 | 1095820 | 2015 | 7 صفحه PDF | دانلود رایگان |
• A polypeptide segment that binds to its target in two distinct conformations.
• Both conformations are populated substantially and have lifetimes of tens of milliseconds.
• Both conformers use the same residues to bind overlapping surfaces in the target.
• The segment could regulate the activity of an adjacent segment.
The Sds3 transcriptional corepressor facilitates the assembly of the 1- to 2-MDa histone deacetylase-associated Sin3L/Rpd3L complex by providing a crucial homodimerization activity. Sds3 engages the scaffolding protein Sin3A, via a bipartite motif within the Sin3 interaction domain (SID) comprising a helix and an extended segment. Here, we show that the SID samples two discrete, substantially populated conformations with lifetimes in the tens of milliseconds range. The two conformations differ via a translation of the main chain and the corresponding side chains in the 5- to 7-Å range. Given the close proximity of the SID to other functional motifs in Sds3 at the sequence level, the conformational exchange has the potential to regulate these activities.
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Journal: Journal of Molecular Biology - Volume 427, Issue 24, 4 December 2015, Pages 3817–3823