Calcium-binding EGF domain | |||||||||
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Identifiers | |||||||||
Symbol | EGF_CA | ||||||||
Pfam | PF07645 | ||||||||
Pfam clan | CL0001 | ||||||||
InterPro | IPR013091 | ||||||||
CDD | cd00054 | ||||||||
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In molecular biology, the calcium-binding EGF domain is an EGF-like domain of about forty amino-acid residues found in epidermal growth factor (EGF). This domain is present in a large number of membrane-bound and extracellular, mostly animal, proteins. [1] [2] [3] [4] [5] Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains. [6] Calcium-binding may be crucial for numerous protein-protein interactions.
For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. [7] The first, third and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated. [6] A conserved aromatic residue, as well as the second conserved negative residue, are thought to be involved in stabilising the calcium-binding site.
As in non-calcium binding EGF-like domains, there are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes. [6]
Calcium-binding EGF domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | EGF_CA | ||||||||
Pfam | PF07645 | ||||||||
Pfam clan | CL0001 | ||||||||
InterPro | IPR013091 | ||||||||
CDD | cd00054 | ||||||||
|
In molecular biology, the calcium-binding EGF domain is an EGF-like domain of about forty amino-acid residues found in epidermal growth factor (EGF). This domain is present in a large number of membrane-bound and extracellular, mostly animal, proteins. [1] [2] [3] [4] [5] Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains. [6] Calcium-binding may be crucial for numerous protein-protein interactions.
For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. [7] The first, third and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated. [6] A conserved aromatic residue, as well as the second conserved negative residue, are thought to be involved in stabilising the calcium-binding site.
As in non-calcium binding EGF-like domains, there are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes. [6]