Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.

doi:10.1021/bi101106x

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Article

Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.

Biochemistry - 5 Oct 2010

Zhan Hongli, Camargo Maricela, Matthews Kathleen S

Abstract excerpt

The central region of the LacI N-subdomain monomer-monomer interface includes residues K84, V94, V95, V96, S97, and M98. The side chains of these residues line the β-strands at this interface and interact to create a network of hydrophobic, charged, and polar interactions that significantly rearranges in different functional states of LacI. Prior work showed that converting K84 to an apolar residue or converting...

Topics

Allosteric Regulation
DNA
Escherichia coli
Escherichia coli Proteins
Lac Repressors
Models, Molecular
Mutation
Protein Binding
Protein Stability
Protein Structure, Tertiary
Protein Unfolding

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Identifiers

PMID: 20804152
DOI: 10.1021/bi101106x
PMCID: PMC3006071

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