Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases
Ruidan Shen, Rory Crean, Keith J. Olsen, Marina Corbella, Ana Rita Calixto, Teisha Richan, Tiago A. S. Brandão, Ryan D. Berry, Alex Tolman, J. Patrick Loria, Sean Johnson, Shina Caroline Lynn Kamerlin, Alvan C. Hengge
Abstract
. The chimeric proteins' WPD-loops differ significantly in their relative stability and rigidity. The time required for interconversion, coupled with electrostatic effects revealed by simulations, likely accounts for the activity differences between chimeras, and relative to the native enzymes. Our results further the understanding of connections between enzyme activity and the dynamics of catalytically important groups, particularly the effects of non-catalytic residues on key conformational equilibria.
Topics & Concepts
Protein tyrosine phosphatasePhosphataseLoop (graph theory)TyrosineSequence (biology)ChemistryBiochemistryCell biologyComputational biologyBiologyPhosphorylationMathematicsCombinatoricsProtein Tyrosine PhosphatasesATP Synthase and ATPases ResearchGalectins and Cancer Biology