Article
A trade between similar but nonequivalent intrasubunit and intersubunit contacts in Cro dimer evolution.
Biochemistry - 23 May 2006
Newlove Tracey, Atkinson Kelly R, Van Dorn Laura O, Cordes Matthew H J
Abstract excerpt
The homodimeric lambda Cro protein has a "ball-and-socket" interface that includes insertion of an aromatic side chain, Phe 58, from each subunit into a cavity in the hydrophobic core of the other subunit. This overlap between the subunit core and dimer interface hypothetically explains the strong dimerization and weak monomer stability of lambda Cro in comparison to homologues. According to a model developed...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
