Gla domain

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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

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].

[edit] Subfamilies

[edit] Human proteins containing this domain

BGLAP; F10; F2; F7; F9; GAS6; MGP; PROC; PROS1; PROZ; PRRG1; PRRG2; PRRG3; PRRG4;

[edit] References

  1. ^ Friedman PA, Przysiecki CT (1987). "Vitamin K-dependent carboxylation". Int. J. Biochem. 19 (1): 1–7. doi:10.1016/0020-711X(87)90116-9. PMID 3106112. 
  2. ^ Vermeer C (1990). "Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase". Biochem. J. 266 (3): 625–636. PMID 2183788. 
  3. ^ 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:10.1073/pnas.84.23.8335. PMID 3317405. 
  4. ^ 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:10.1074/jbc.270.14.7980. PMID 7713897. 
  5. ^ 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:10.1074/jbc.271.27.16227. PMID 8663165. 
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