Abstract:
:Molecular modeling is used to demonstrate that the major structural deformations of DNA caused by four different minor groove binding proteins, TBP, SRY, LEF-1, and PurR, can all be mimicked by stretching the double helix between two 3'-phosphate groups flanking the binding region. This deformation reproduces the widening of the minor groove and the overall bending and unwinding of DNA caused by protein binding. It also reproduces the principal kinks associated with partially intercalated amino acid side chains, observed with such interactions. In addition, when protein binding involves a local transition to an A-like conformation, phosphate neutralization, via the formation of protein-DNA salt bridges, appears to favor the resulting deformation.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Lebrun A,Lavery Rdoi
10.1002/(SICI)1097-0282(19990415)49:5<341::AID-BIPsubject
Has Abstractpub_date
1999-04-15 00:00:00pages
341-53issue
5eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(19990415)49:5<341::AID-BIPjournal_volume
49pub_type
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