Sandbox 16: Difference between revisions
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== Structure == | == Structure == | ||
The <scene name='Sandbox_16/Alp-1/2'>secondary structure</scene> contains the double β-barrel motif (colored yellow) that is characteristic of the chymotrypsin family as well as an active site containing the <scene name='Sandbox_16/Alp-1/ | The <scene name='Sandbox_16/Alp-1/2'>secondary structure</scene> contains the double β-barrel motif (colored yellow) that is characteristic of the chymotrypsin family as well as an active site containing the <scene name='Sandbox_16/Alp-1/6'>"catalytic triad"</scene> - His 57, Asp 102, and Ser 195 - that is responsible for proteolysis. The preference for αlp to cleave substrates on the C-terminal side of small hydrophobic residues, such as Alanine and Valine is mostly due to <scene name='Sandbox_16/Alp-1/3'>three residues in the S1 pocket</scene> consisting of Met 190, Met 213, and Val 218<ref>PMID:9232638</ref>. | ||
== References == | == References == | ||
<references/> | <references/> | ||
