User:Christopher French: Difference between revisions

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Caspase 8 is a 58 kilodalton protein that shares similarities with other members of the caspase family. The protein is composed of two subunits, referred to as <scene name='User:Christopher_French/Subunits/1'>p18 and p11</scene>. These two subunits form a heterodimer. The protein has a α/ß folding motif that has a central six stranded beta sheet. Five of the strands are parallel and one is anti-parallel. The antiparallel strand is on the edge of the ß sheet. There are also six alpha helices in the protein structure. Three of these alpha helices are located on one side of the ß sheet and the other two on the other side, forming a <scene name='User:Christopher_French/Secondary_structure/3'>three layer sandwich</scene>. The p18 subunit has a Rossmann fold. There is a <scene name='User:Christopher_French/Turn_of_helix/2'>turn of helix</scene>(α1’) which is part of a large loop (loop 1). This is along the binding pocket region of the p18 subunit. There is a two-stranded antiparallel ß sheet found at the top of the main ß sheet which forms the base of the binding pocket (4,5).

Caspase 8 is a 58 kilodalton protein that shares similarities with other members of the caspase family. The protein is composed of two subunits, referred to as <scene name='User:Christopher_French/Subunits/1'>p18 and p11</scene>. These two subunits form a heterodimer. The protein has a α/ß folding motif that has a <scene name='User:Christopher_French/B-sheets/1'>central six stranded beta sheet</scene>. Five of the strands are parallel and one is anti-parallel. The antiparallel strand is on the edge of the ß sheet. There are also six alpha helices in the protein structure. Three of these alpha helices are located on one side of the ß sheet and the other two on the other side, forming a <scene name='User:Christopher_French/Secondary_structure/3'>three layer sandwich</scene>. The p18 subunit has a Rossmann fold. There is a <scene name='User:Christopher_French/Turn_of_helix/2'>turn of helix</scene>(α1’) which is part of a large loop (loop 1). This is along the binding pocket region of the p18 subunit. There is a two-stranded antiparallel ß sheet found at the top of the main ß sheet which forms the base of the binding pocket (4,5).

User:Christopher French: Difference between revisions

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Revision as of 19:31, 27 April 2009 view source Christopher French (talk \| contribs) 42 edits No edit summary ← Older edit		Revision as of 22:01, 27 April 2009 view source Christopher French (talk \| contribs) 42 edits No edit summary Newer edit →
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	Caspase 8 is a 58 kilodalton protein that shares similarities with other members of the caspase family. The protein is composed of two subunits, referred to as <scene name='User:Christopher_French/Subunits/1'>p18 and p11</scene>. These two subunits form a heterodimer. The protein has a α/ß folding motif that has a central six stranded beta sheet. Five of the strands are parallel and one is anti-parallel. The antiparallel strand is on the edge of the ß sheet. There are also six alpha helices in the protein structure. Three of these alpha helices are located on one side of the ß sheet and the other two on the other side, forming a <scene name='User:Christopher_French/Secondary_structure/3'>three layer sandwich</scene>. The p18 subunit has a Rossmann fold. There is a <scene name='User:Christopher_French/Turn_of_helix/2'>turn of helix</scene>(α1’) which is part of a large loop (loop 1). This is along the binding pocket region of the p18 subunit. There is a two-stranded antiparallel ß sheet found at the top of the main ß sheet which forms the base of the binding pocket (4,5).		Caspase 8 is a 58 kilodalton protein that shares similarities with other members of the caspase family. The protein is composed of two subunits, referred to as <scene name='User:Christopher_French/Subunits/1'>p18 and p11</scene>. These two subunits form a heterodimer. The protein has a α/ß folding motif that has a <scene name='User:Christopher_French/B-sheets/1'>central six stranded beta sheet</scene>. Five of the strands are parallel and one is anti-parallel. The antiparallel strand is on the edge of the ß sheet. There are also six alpha helices in the protein structure. Three of these alpha helices are located on one side of the ß sheet and the other two on the other side, forming a <scene name='User:Christopher_French/Secondary_structure/3'>three layer sandwich</scene>. The p18 subunit has a Rossmann fold. There is a <scene name='User:Christopher_French/Turn_of_helix/2'>turn of helix</scene>(α1’) which is part of a large loop (loop 1). This is along the binding pocket region of the p18 subunit. There is a two-stranded antiparallel ß sheet found at the top of the main ß sheet which forms the base of the binding pocket (4,5).
	{{STRUCTURE_1qtn \| PDB=1qtn \| SCENE= }}		{{STRUCTURE_1qtn \| PDB=1qtn \| SCENE= }}