1995
DOI: 10.1021/bi00008a004
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Abstract: Selectively labeled polypeptides comprising the gamma-carboxyglutamic acid (Gla) domain (GD) and helical stack (HS) regions of human protein C (PC), and consisting of amino acid residues 1-47, have been chemically synthesized and their Ca2+ binding properties assessed by [13C]-NMR methods. A total of nine such polypeptides have been studied, each containing one of the Gla residues fully enriched with [13C] at its two gamma-carboxylate carbon atoms. Additions of Ca2+ resulted in readily measurable [13C] chemica… Show more

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Cited by 22 publications
(17 citation statements)
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References 31 publications
(53 reference statements)
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“…A conceivable explanation is that Ca 2+ ‐binding sites in the Gla domain play a role in the Ca 2+ ‐dependent fVIIa activity in the presence of sTF, i.e. in sTF binding, considering the broad range of affinities represented within this group of sites [37]. These sites have been hypothesized to be important for the expression of TF‐interactive epitopes [38].…”
Section: Discussionmentioning
confidence: 99%
“…A conceivable explanation is that Ca 2+ ‐binding sites in the Gla domain play a role in the Ca 2+ ‐dependent fVIIa activity in the presence of sTF, i.e. in sTF binding, considering the broad range of affinities represented within this group of sites [37]. These sites have been hypothesized to be important for the expression of TF‐interactive epitopes [38].…”
Section: Discussionmentioning
confidence: 99%
“…In contrast, factor VIIa binding to phospholipid and F1 A2 could not be induced by Mgz'. Applying prothrombin and protein C as models for the Gla domain of factor VIIa, presumably Mg" can not replace Ca" in the interior binding sites, corresponding to Ca" ions 2-5 in the Ca2'~ structure of prothrombin fragment 1, and/or replace the solvent-accessible Ca2+ ions (1, 6 and 7 ; Soriano-Garcia et al, 1992), presumably Ca6, required for phospholipid binding (Colpitts et al, 1995). By comparison of the apo and Ca'+ structures of the factor X Gla domain, it was seen that buried Ca2+ ions occupy the space that harbours the membrane-interactive residues Phe4, Leu5 and Val8 in the apo structure and it was suggested that the binding of these Caz+ ions brings about the phospholipid accessibility of those three residues (Sunnerhagen et al, 1995).…”
Section: Discussionmentioning
confidence: 99%
“…Gla residues were originally identified in the vitamin K-dependent blood-clotting factors including prothrombin. Subsequently they were found in other vertebrate proteins such as osteocalcin (calcium-binding protein) (10,11) and have been implicated in Ca 2ϩ binding (12,13). The discovery of Gla residues in several Conus peptides has established that this posttranslational modification has a much wider phylogenetic distribution than previously thought (14).…”
Section: or Mg 2؉ )mentioning
confidence: 99%