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User:Amy Kerzmann/Sandbox 5
From Proteopedia
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The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/4' target='2'>elastase binding pocket</scene> contains <font color="#808080">Gly190</font>, <font color="#008000">Val216</font> and <font color="#FFA500">Thr226</font>. | The <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/4' target='2'>elastase binding pocket</scene> contains <font color="#808080">Gly190</font>, <font color="#008000">Val216</font> and <font color="#FFA500">Thr226</font>. | ||
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| + | By highlighting the solvent-accessible surfaces of <scene name='User:Amy_Kerzmann/Sandbox_5/Trypsin-wt-triad/3' target='1'>trypsin</scene> and <scene name='User:Amy_Kerzmann/Sandbox_5/Elastase-triad/5 target='2''>elastase</scene>, one can better understand why trypsin has specificity for large, charged sidechains whereas elastase targets smaller residues. | ||
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Revision as of 09:36, 10 February 2010
Serine Proteases
The most famous members of the serine protease family are trypsin, chymotrypsin and elastase. These digestive enzymes are also useful tools in biochemistry and molecular biology to ascertain protein sequences.
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Serine proteases perform their catalytic roles using three key residues: Ser, His, Asp. Because the proteases utilize these three residues for function, they are referred to as the catalytic triad. Highlight the . Mouse over the structure to determine the residue numbers for Ser, Asp and His.
Now compare chymotrypsin to . The .
The contains Asp189 to select for positively charged sidechains.
The contains Gly190, Val216 and Thr226.
By highlighting the solvent-accessible surfaces of and , one can better understand why trypsin has specificity for large, charged sidechains whereas elastase targets smaller residues.
