Sandbox Reserved 1482: Difference between revisions
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Factor VIII protein is composed of six globular domains: A<sub>1</sub>-A<sub>2</sub>-B-A<sub>3</sub>-C<sub>1</sub>-C<sub>2</sub> and contains one Ca<sup>2+</sup> and two Cu<sup>2+</sup> ions. It has a molecular weight of 330 kDa <ref name="Ngo" /><ref name="El" /><ref name="uni" />. | Factor VIII protein is composed of six globular domains: A<sub>1</sub>-A<sub>2</sub>-B-A<sub>3</sub>-C<sub>1</sub>-C<sub>2</sub> and contains one Ca<sup>2+</sup> and two Cu<sup>2+</sup> ions. It has a molecular weight of 330 kDa <ref name="Ngo" /><ref name="El" /><ref name="uni" />. | ||
The three A domains are homologous to the A domains of the copper-binding protein | The three A domains are homologous to the A domains of the copper-binding protein [[Ceruloplasmin]] <ref name="wikipedia" /><ref name="El" />. Together, they form a triangular heterotrimer where the A<sub>1</sub> and A<sub>3</sub> domains interact with the C<sub>2</sub> and C<sub>1</sub> domains, respectively <ref name="Ngo" />. | ||
The C domains belong to the phospholipid-binding discoidin domain family <ref name="wikipedia" />. They are adjacent at the base of the triangular heterotrimer. Moreover, C<sub>1</sub> and C<sub>2</sub> domains are structurally homologous and they have the ability to bind the membrane. Indeed, both C domain protrude three β-hairpin loops with hydrophobic and basic residues in the same direction. Thanks to these loops the factor VIII might interact with the phospholipid bilayer. <ref name="Ngo" /> | The C domains belong to the phospholipid-binding discoidin domain family <ref name="wikipedia" />. They are adjacent at the base of the triangular heterotrimer. Moreover, C<sub>1</sub> and C<sub>2</sub> domains are structurally homologous and they have the ability to bind the membrane. Indeed, both C domain protrude three β-hairpin loops with hydrophobic and basic residues in the same direction. Thanks to these loops the factor VIII might interact with the phospholipid bilayer. <ref name="Ngo" /> | ||