Sandbox Reserved 348: Difference between revisions
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{{ STRUCTURE_1ppb | PDB=1ppb | SCENE=Sandbox_Reserved_348/Ligand/ | {{ STRUCTURE_1ppb | PDB=1ppb | SCENE=Sandbox_Reserved_348/Ligand/2 }} | ||
[[Image: | [[Image:Thrombin_in_Coagulation.png|thumb|left|300px|The role of thrombin and prothrombin in [http://en.wikipedia.org/wiki/Coagulation coagulation].]] | ||
Thrombin is a [[trypsin]]-like [[Serine Protease|serine protease]] which is best known for its role in blood clotting. In humans, the F2 gene codes for prothrombin, which is also known as Coagulation Factor II.<ref name="Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively.">PMID:3474786</ref><ref name="Nucleotide sequence of the gene for human prothrombin.">PMID:2825773</ref> Clevage of prothrombin to form activated α-thrombin is a key step in the final common pathway of blood clotting, because thrombin activates fibrin, which creates cross-linked fibrin clots.<ref name="Thrombin interactions.">PMID:12970119</ref> | Thrombin is a [[trypsin]]-like [[Serine Protease|serine protease]] which is best known for its role in blood clotting. In humans, the F2 gene codes for prothrombin, which is also known as Coagulation Factor II.<ref name="Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively.">PMID:3474786</ref><ref name="Nucleotide sequence of the gene for human prothrombin.">PMID:2825773</ref> Clevage of prothrombin to form activated α-thrombin is a key step in the final common pathway of blood clotting, because thrombin activates fibrin, which creates cross-linked fibrin clots.<ref name="Thrombin interactions.">PMID:12970119</ref> | ||
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==Structure== | |||
== | Thrombin is comprised of two chains, often referred to as the <scene name='Sandbox_Reserved_348/Small_subunit/2'>short chain</scene> and the <scene name='Sandbox_Reserved_348/Large_subunit/2'>long chain</scene>. There is one <scene name='Sandbox_Reserved_348/Ligand/2'>active site</scene>, which in the case of [[1ppb]] is occupied with D-Phe-Pro-Arg chloromethylketone.<ref name="The refined 1.9A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.">PMID:2583108</ref> Additionally, there are three structural disulfide bonds. | ||
==3D Structures of α-Thrombin== | ==3D Structures of α-Thrombin== | ||
