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| Anchoring of Coagulation factor VIIa to the membrane through its GLA domain | ||
| Identifiers | ||
|---|---|---|
| Symbol | Gla | |
| Pfam | PF00594 | |
| InterPro | IPR000294 | |
| PROSITE | PDOC00011 | |
| SCOP | 1cfi | |
| OPM family | 97 | |
| OPM protein | 1pfx | |
| Available PDB structures:
1q8hA:6-47 1q3mA:57-98 1vzmB:53-93 1nl1A:49-90 2spt :49-90 1nl2A:49-90 2pf1 :79-90 1nl8L:45-86 1p0sL:45-86 1whf :45-86 1whe :45-86 1iodG:45-84 1j34C:6-46 1j35C:6-46 1pfxL:8-48 1cfi :52-93 1cfh :52-93 1mgx :52-93 1nl0G:52-91 1lqvC:47-75 1wv7L:65-106 1wqvL:65-106 1wssL:65-106 1w0yL:65-106 1z6jL:65-106 1fakL:65-106 1wunL:65-106 1wtgL:65-106 1danL:65-106 |
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Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain is a protein domain that contains post-translational modifications of many glutamate residues by vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla). The Gla residues are responsible for the high-affinity binding of calcium ions [1][2].
The GLA domain is responsible for the high-affinity binding of calcium ions. It starts at the N-terminal extremity of the mature form of proteins and ends with a conserved aromatic residue; a conserved Gla-x(3)-Gla-x-Cys motif[3] is found in the middle of the domain which seems to be important for substrate recognition by the carboxylase.
The 3D structures of several Gla domains have been solved[4][5]. Calcium ions induce conformational changes in the Gla domain and are necessary for the Gla domain to fold properly. A common structural feature of functional Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane[5].
Subfamilies
- Coagulation factor, Gla region IPR002383
Human proteins containing this domain
BGLAP; F10; F2; F7; F9; GAS6; MGP; PROC; PROS1; PROZ; PRRG1; PRRG2; PRRG3; PRRG4;
References
- ^ Friedman PA, Przysiecki CT (1987). "Vitamin K-dependent carboxylation". Int. J. Biochem. 19 (1): 1–7. doi:. PMID 3106112.
- ^ Vermeer C (1990). "Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase". Biochem. J. 266 (3): 625–636. PMID 2183788.
- ^ Price PA, Fraser JD, Metz-Virca G (1987). "Molecular cloning of matrix Gla protein: implications for substrate recognition by the vitamin K-dependent gamma-carboxylase". Proc. Natl. Acad. Sci. U.S.A. 84 (23): 8335–8339. doi:. PMID 3317405.
- ^ Freedman SJ, Furie BC, Furie B, Baleja JD (1995). "Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy". J. Biol. Chem. 270 (14): 7980–7987. doi:. PMID 7713897.
- ^ a b Freedman SJ, Furie BC, Furie B, Baleja JD, Blostein MD, Jacobs M (1996). "Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX". J. Biol. Chem. 271 (27): 16227–16236. doi:. PMID 8663165.
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