Sandbox Reserved 348: Difference between revisions

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{{Template:Sandbox_Reserved_BCMB307}}
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{{ STRUCTURE_1ppb | PDB=1ppb | SCENE=Sandbox_Reserved_348/Ligand/4 }}
[[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]] 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 clevage by thrombin activates several factors in blood clotting, especially [[fibrin]], [[factor XIII]], and [[protein C]].<ref name="Thrombin interactions.">PMID:12970119</ref>


{{ STRUCTURE_1ppb | PDB=1ppb | SCENE=Sandbox_Reserved_348/Cpk/1 }}
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=Section 1=
==Structure==
<scene name='Sandbox_Reserved_348/Raw/1'>Raw Scene</scene>
Thrombin is comprised of two chains, often referred to as the <scene name='Sandbox_Reserved_348/Small_subunit/3'>short chain</scene> and the <scene name='Sandbox_Reserved_348/Large_subunit/3'>long chain</scene>.  All known functional epitopes are found on the long chain.  There is one active site, which in the case of [[1ppb]] is occupied with <scene name='Sandbox_Reserved_348/Ligand/4'>D-Phe-Pro-Arg chloromethylketone</scene>.<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.
=Section 2=
{|
<scene name='Sandbox_Reserved_348/Cpk/1'>CPK</scene>
|While thrombin is described as a [[trypsin]]-like [[serine protease]], it is more specific than trypsin due to two exosites which bind the substrate at a point separate from the active site.  These exosites also allow for more specific inhibition, since [[protein C]] and [[factor Xa]] have similar active sites but play very different roles in the clotting process.<ref name="Thrombin interactions."/>
=Section 3=
|[[Image:Thrombin_catalytic_triad.png|thumb|left|150px|The [[serine protease]] catalytic triad in the active site of α-thrombin, bound to D-Phe-Pro-Arg chloromethylketone ligand.]]
[[Image:1ppb.png|300px|This are a caption.]]
|}
 
==Regulation==
{|
|[[Image:Thrombin-Hirudin_Complex.png|thumb|left|200px|<scene name='Sandbox_Reserved_348/Hirudin/2'>α-Thrombin - Hirudin Complex</scene>]]
|Prothrombin is proteolytically activated to α-thrombin by [[factor Xa]].  α-Thrombin is permanently inactivated by the [[Serine Protease Inhibitor]] [[antithrombin]], with [[heparin]] as a cofactor, and allosterically regulated by sodium ion concentration.  [[Thrombomodulin]] inhibits clevage of fibrinogen to fibrin, but also enhances α-thrombin activity with respect to [[protein C]].  Since activated protein C proteolytically inactivates earlier steps in the chain, this effectively reverses the role of thrombin from coagulant to anticoagulant.<ref name="Thrombin interactions."/>
 
[[Hirudin]] is a potent natural inhibitor of thrombin, produced by [http://en.wikipedia.org/wiki/Leeches leeches] such as <I>[http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]</I>.
|}
==3D Structures==
===α-Thrombin===
*[[1ppb]]
*[[1uma]]
*[[1de7]]
 
===Prothrombin===
*[[2afq]]
 
==See Also==
*[[Fibrin]]
*[[Trypsin]]
*[[Serine Protease]]
*[[Factor Xa]]
*[[Hirudin]]
 
==External Resources==
*[http://en.wikipedia.org/wiki/Thrombin Thrombin] at Wikipedia
*[http://en.wikipedia.org/wiki/Serine_protease Serine protease] at Wikipedia
*[http://en.wikipedia.org/wiki/Fibrin_glue Fibrin Glue] at Wikipedia
*[http://en.wikipedia.org/wiki/Coagulation Coagulation] (blood clotting) at Wikipedia
*[http://en.wikipedia.org/wiki/Hemophilia Hemophilia] at Wikipedia


<ref name="Placeholder">PMID:2583108</ref>
=References=
=References=
<references/>
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