IndraLab

Statements


| 3

sparser
"Based on the available crystal structures, with such a short DNA duplex it is difficult to rationalize how Rap1 DBD would be able to bind with both Myb-like domains interacting with the DNA."

sparser
"The double-stranded part of the telomere is bound by Rap1 (repressor/activator-site binding protein) through its Myb-like domain, which in turn causes nucleation of a protein complex by recruiting, th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"The transient opening of the wrapping loop destabilizes this clamped structure and allows Rap1 binding to DNA through a single Myb-like domain [ xref , xref ]."