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ABSTRACT: Background
The small family of vitamin K-dependent proteins are characterized by posttranslational modification of specific glutamic acid residues to yield γ-carboxyglutamic acid (Gla). Gla residues give these proteins calcium ion-binding properties, which are essential for a number of coagulation factors and mineralization processes. Biophysical characteristics of Gla are, however, incomplete, hindering molecular dynamics simulations and protein structure predictions.Objectives
This study aimed to elucidate the general biophysical characteristics (pK a and K D) of calcium binding to γ-carboxyglutamic acid in a protein environment and determine how positioning of γ-carboxyglutamic acid influences cooperative calcium binding and protein st
SUBMITTER: Ippel H
PROVIDER: S-EPMC12312033 | biostudies-literature | 2025 Jul
REPOSITORIES: biostudies-literature