Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix.
about
Amino acid positions subject to multiple coevolutionary constraints can be robustly identified by their eigenvector network centrality scoresData on publications, structural analyses, and queries used to build and utilize the AlloRep database.Comparing the functional roles of nonconserved sequence positions in homologous transcription repressors: implications for sequence/function analyses.Functionally important positions can comprise the majority of a protein's architecture.Identification of a small-molecule inhibitor of bacterial AraC family activators.Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox Proteins.Novel insights from hybrid LacI/GalR proteins: family-wide functional attributes and biologically significant variation in transcription repression.Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor proteinSubdividing repressor function: DNA binding affinity, selectivity, and allostery can be altered by amino acid substitution of nonconserved residues in a LacI/GalR homologue.Experimental identification of specificity determinants in the domain linker of a LacI/GalR protein: bioinformatics-based predictions generate true positives and false negatives.Using Evolution to Guide Protein Engineering: The Devil IS in the Details.Tetramer opening in LacI-mediated DNA looping.Mispair-specific recruitment of the Mlh1-Pms1 complex identifies repair substrates of the Saccharomyces cerevisiae Msh2-Msh3 complex.Functional consequences of exchanging domains between LacI and PurR are mediated by the intervening linker sequence.In vivo tests of thermodynamic models of transcription repressor function.Mechanics of DNA bridging by bacterial condensin MukBEF in vitro and in singulo.Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.Computational predictors fail to identify amino acid substitution effects at rheostat positions.Lactose Repressor Hinge Domain Independently Binds DNA.Sliding of a single lac repressor protein along DNA is tuned by DNA sequence and molecular switching.
P2860
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P2860
Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 2006
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Extrinsic interactions dominat ...... repressor protein hinge helix.
@en
Extrinsic interactions dominat ...... repressor protein hinge helix.
@nl
type
label
Extrinsic interactions dominat ...... repressor protein hinge helix.
@en
Extrinsic interactions dominat ...... repressor protein hinge helix.
@nl
prefLabel
Extrinsic interactions dominat ...... repressor protein hinge helix.
@en
Extrinsic interactions dominat ...... repressor protein hinge helix.
@nl
P2093
P2860
P356
P1433
P1476
Extrinsic interactions dominat ...... repressor protein hinge helix.
@en
P2093
Hongli Zhan
Kathleen Shive Matthews
Liskin Swint-Kruse
P2860
P304
P356
10.1021/BI052619P
P407
P577
2006-05-01T00:00:00Z