Factor Xa: Difference between revisions

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The factor Xa heavy chain contains the activation peptide (no crystal structures of inactive Factor X containing the activation peptide have been solved) and the trypsin-like serine protease domain

The members of the trypsin-like serine protease family have two homologous greek key β-barrel subdomains (<scene name='Factor_Xa/Transparent_-no_inhib-_barrel1/1'>barrel 1</scene>, <scene name='Factor_Xa/Transparent_-_no_inhib_barrel2/1'>barrel 2</scene>) in the heavy chain. The greek key barrel is characterized as an up and down β-barrel with an n+3 linkage across the barrel, in this case, the across barrel linkage is an α-helix. The <scene name='Factor_Xa/Transparent_-no_inhib-_barrels/1'>two barrels</scene> pack together asymmetrically to constitute the compact catalytic domain. The subdomain interface forms the active site with the substrate binding cleft running along the subdomain boundary. Notably, the conserved catalytic tetrad residues Ser195, His57, Asp102, and Ser214 are from the C-, N-, N-, and C-terminal domains, respectively. Although the hydrophobic core structures remain conserved throughout the family (12), considerable variation is seen in the surface loops, especially surrounding the active site where they determine substrate specificities

The members of the trypsin-like serine protease family have two homologous greek key β-barrel subdomains (<scene name='Factor_Xa/Transparent_-no_inhib-_barrel1/1'>barrel 1</scene>, <scene name='Factor_Xa/Transparent_-_no_inhib_barrel2/1'>barrel 2</scene>) in the heavy chain. The greek key barrel is characterized as an up and down β-barrel with an n+3 linkage across the barrel, in this case, the across barrel linkage is an α-helix. The <scene name='Factor_Xa/Transparent_-no_inhib-_barrels/1'>two barrels</scene> pack together asymmetrically to constitute the compact <scene name='Factor_Xa/Transparent_-_barrels_catalyt/1'>catalytic domain</scene>. The subdomain interface forms the active site with the substrate binding cleft running along the subdomain boundary. Notably, the conserved catalytic tetrad residues Ser195, His57, Asp102, and Ser214 are from the C-, N-, N-, and C-terminal domains, respectively. Although the hydrophobic core structures remain conserved throughout the family (12), considerable variation is seen in the surface loops, especially surrounding the active site where they determine substrate specificities

Factor Xa: Difference between revisions

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Revision as of 17:47, 16 April 2011 view source Jacqueline Gertz (talk \| contribs) 254 edits →Heavy Chain ← Older edit		Revision as of 17:50, 16 April 2011 view source Jacqueline Gertz (talk \| contribs) 254 edits →Heavy Chain Newer edit →
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	The factor Xa heavy chain contains the activation peptide (no crystal structures of inactive Factor X containing the activation peptide have been solved) and the trypsin-like serine protease domain		The factor Xa heavy chain contains the activation peptide (no crystal structures of inactive Factor X containing the activation peptide have been solved) and the trypsin-like serine protease domain

	The members of the trypsin-like serine protease family have two homologous greek key β-barrel subdomains (<scene name='Factor_Xa/Transparent_-no_inhib-_barrel1/1'>barrel 1</scene>, <scene name='Factor_Xa/Transparent_-_no_inhib_barrel2/1'>barrel 2</scene>) in the heavy chain. The greek key barrel is characterized as an up and down β-barrel with an n+3 linkage across the barrel, in this case, the across barrel linkage is an α-helix. The <scene name='Factor_Xa/Transparent_-no_inhib-_barrels/1'>two barrels</scene> pack together asymmetrically to constitute the compact catalytic domain. The subdomain interface forms the active site with the substrate binding cleft running along the subdomain boundary. Notably, the conserved catalytic tetrad residues Ser195, His57, Asp102, and Ser214 are from the C-, N-, N-, and C-terminal domains, respectively. Although the hydrophobic core structures remain conserved throughout the family (12), considerable variation is seen in the surface loops, especially surrounding the active site where they determine substrate specificities		The members of the trypsin-like serine protease family have two homologous greek key β-barrel subdomains (<scene name='Factor_Xa/Transparent_-no_inhib-_barrel1/1'>barrel 1</scene>, <scene name='Factor_Xa/Transparent_-_no_inhib_barrel2/1'>barrel 2</scene>) in the heavy chain. The greek key barrel is characterized as an up and down β-barrel with an n+3 linkage across the barrel, in this case, the across barrel linkage is an α-helix. The <scene name='Factor_Xa/Transparent_-no_inhib-_barrels/1'>two barrels</scene> pack together asymmetrically to constitute the compact <scene name='Factor_Xa/Transparent_-_barrels_catalyt/1'>catalytic domain</scene>. The subdomain interface forms the active site with the substrate binding cleft running along the subdomain boundary. Notably, the conserved catalytic tetrad residues Ser195, His57, Asp102, and Ser214 are from the C-, N-, N-, and C-terminal domains, respectively. Although the hydrophobic core structures remain conserved throughout the family (12), considerable variation is seen in the surface loops, especially surrounding the active site where they determine substrate specificities