Sandbox Reserved 1493: Difference between revisions
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Most ligands of integrin αIIbβ3 share the particularity of having at least one RGD pattern in their protein sequence that can be recognized by the RGD binding site in the β3 subunit. | Most ligands of integrin αIIbβ3 share the particularity of having at least one RGD pattern in their protein sequence that can be recognized by the RGD binding site in the β3 subunit. | ||
[[Image:Binding_sites.png|thumb|right|Domains and ligand binding sites of integrin αIIbβ3]] | |||
=== Cation binding sites === | === Cation binding sites === | ||
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Unlike fibrinogen or von Willebrand factors, some proteins such as collagen have hidden RGD sequences which are only exposed after cleavage or protein denaturation. Still, collagen contains multiple KGD motifs (12 KGD motifs in the α-chains of the COL15 domain of collagen XVII). This pattern can be recognized by the KGD binding site of the β3 subunit | Unlike fibrinogen or von Willebrand factors, some proteins such as collagen have hidden RGD sequences which are only exposed after cleavage or protein denaturation. Still, collagen contains multiple KGD motifs (12 KGD motifs in the α-chains of the COL15 domain of collagen XVII). This pattern can be recognized by the KGD binding site of the β3 subunit | ||
== Activity modulation == | == Activity modulation == | ||
