User:Cody Couperus/Sandbox 1: Difference between revisions

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'''Exosite I''' is located on the B chain and had both basic and hydrophobic character. It is important in binding <scene name='58/583418/Fibrinogen/1'>fibrinogen</scene>, platelet activated receptors, and <scene name='58/583418/Thrombomodulin/1'>thrombomodulin</scene>.

'''Exosite II''' is also part of the B chain, and derived from numerous basic amino acids, this is the site of heparin binding through the sulfate groups on the glycosaminoglycan. It is also the site of GpIα on the platelet surface.

'''Exosite II''' is also part of the B chain, and derived from numerous basic amino acids, this is the site of <scene name='58/583418/Antithrombin/1'>heparin binding</scene> through the sulfate groups on the glycosaminoglycan. It is also the site of GpIα on the platelet surface.

The <scene name='58/583418/Sodium_binding_loop/1'>sodium binding site</scene> is formed by the 180s- and 220s- loops. Na+ is bound by the backbone oxygens of Arg221a and Lys224 in addition to four water molecules in a classic [http://chemwiki.ucdavis.edu/Inorganic_Chemistry/Crystal_Field_Theory/High_Spin_and_Low_Spin_Complexes#Octahedral_Geometry octahedral geometry]<ref>PMID: 9108691</ref>. Through the covelent disulfide linkage between Cys220 and Cys 191 the sodium binding site is linked to Ser195 and the oxyanion hole.

@@ Line 66: / Line 66: @@
 '''Exosite I''' is located on the B chain and had both basic and hydrophobic character. It is important in binding <scene name='58/583418/Fibrinogen/1'>fibrinogen</scene>, platelet activated receptors, and <scene name='58/583418/Thrombomodulin/1'>thrombomodulin</scene>.
-'''Exosite II''' is also part of the B chain, and derived from numerous basic amino acids, this is the site of heparin binding through the sulfate groups on the glycosaminoglycan. It is also the site of GpIα on the platelet surface.
+'''Exosite II''' is also part of the B chain, and derived from numerous basic amino acids, this is the site of <scene name='58/583418/Antithrombin/1'>heparin binding</scene> through the sulfate groups on the glycosaminoglycan. It is also the site of GpIα on the platelet surface.
 The <scene name='58/583418/Sodium_binding_loop/1'>sodium binding site</scene> is formed by the 180s- and 220s- loops. Na+ is bound by the backbone oxygens of Arg221a and Lys224 in addition to four water molecules in a classic [http://chemwiki.ucdavis.edu/Inorganic_Chemistry/Crystal_Field_Theory/High_Spin_and_Low_Spin_Complexes#Octahedral_Geometry octahedral geometry]<ref>PMID: 9108691</ref>. Through the covelent disulfide linkage between Cys220 and Cys 191 the sodium binding site is linked to Ser195 and the oxyanion hole.