M
Mark A. Wall
Researcher at University of Texas Southwestern Medical Center
Publications - 8
Citations - 2511
Mark A. Wall is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Protein structure & G protein-coupled receptor. The author has an hindex of 8, co-authored 8 publications receiving 2433 citations. Previous affiliations of Mark A. Wall include Howard Hughes Medical Institute.
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Journal ArticleDOI
The structure of the G protein heterotrimer Giα1β1γ2
Mark A. Wall,David E. Coleman,Ethan Lee,Jorge A. Iñiguez-Lluhi,Bruce A. Posner,Alfred G. Gilman,Stephen R. Sprang +6 more
TL;DR: The structure of the G protein heterotrimer Gi alpha 1(GDP)beta 1 gamma 2 (at 2.3 A) reveals two nonoverlapping regions of contact between alpha and beta, an extended interface between beta and nearly all of gamma, and limited interaction of alpha with gamma as mentioned in this paper.
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Evolutionarily conserved networks of residues mediate allosteric communication in proteins
TL;DR: A sequence-based statistical method for quantitatively mapping the global network of amino acid interactions in a protein, which suggests that evolutionarily conserved sparse networks of amino Acid interactions represent structural motifs for allosteric communication in proteins.
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The structural basis for red fluorescence in the tetrameric GFP homolog DsRed.
TL;DR: The 1.9 Å crystal structure of DsRed, a red fluorescent protein from Discosoma coral, is reported, revealing the chemical basis for the functional properties of red fluorescent proteins and provides the basis for rational engineering of this subfamily of GFP homologs.
Journal ArticleDOI
Structural basis of activity and subunit recognition in G protein heterotrimers
TL;DR: The Gly203-->Ala mutant of Gialpha1 binds and hydrolyzes GTP normally but does not dissociate from Gbetagamma, demonstrating that GTP binding and activation can be uncoupled.
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Dynamic Scaffolding in a G Protein-Coupled Signaling System
TL;DR: These studies demonstrate a conformational switch mechanism for PDZ domain function and suggest that INAD behaves more like a dynamic machine rather than a passive scaffold, regulating signal transduction at the millisecond timescale through cycles of conformational change.