1995
DOI: 10.1021/bi00008a004 View full text |Buy / Rent full text
|
|

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

Help me understand this report

Search citation statements

Order By: Relevance
Select...
2
1
1
1
1
16
0

Year Published

1995
1995
2009
2009

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

1
16
0
Order By: Relevance
“…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
Create an account to read the remaining citation statements from this report. You will also get access to:
  • Search over 1b+ citation statments to see what is being said about any topic in the research literature
  • Advanced Search to find publications that support or contrast your research
  • Citation reports and visualizations to easily see what publications are saying about each other
  • Browser extension to see Smart Citations wherever you read research
  • Dashboards to evaluate and keep track of groups of publications
  • Alerts to stay on top of citations as they happen
  • Automated reference checks to make sure you are citing reliable research in your manuscripts
  • 14 day free preview of our premium features.

Trusted by researchers and organizations around the world

Over 100,000 students researchers, and industry experts at use scite

See what students are saying

rupbmjkragerfmgwileyiopcupepmcmbcthiemesagefrontiersapsiucrarxivemeralduhksmucshluniversity-of-gavle
“…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
“…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
“…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