Sandbox 39: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 35: | Line 35: | ||
== Active Site == | == Active Site == | ||
Papain has a broad specificity for protein substrates. The active site consists of seven subsites that can each accommodate one amino acid residue of a substrate. Specificity is controlled, however, by the <scene name='Sandbox_39/Catalytic_triad/1'>catalytic triad</scene>, a hydrophobic pocket that accommodates the side chains of the protein substrate. This triad consists of a histidine, asparagine, and a cysteine, after which the protein is categorized as a cysteine protease. Papain exhibits specific substrate preferences for hydrophobic or aromatic residues. | Papain has a broad specificity for protein substrates. The active site consists of seven subsites (S1-S4 and S1’-S3’) that can each accommodate one amino acid residue of a protein substrate (P1-P4 and P1’-P3’). | ||
[[Image:Subsites.jpg|left]] | |||
Specificity is controlled, however, by the <scene name='Sandbox_39/Catalytic_triad/1'>catalytic triad</scene>, a hydrophobic pocket that accommodates the side chains of the protein substrate. This triad consists of a histidine, asparagine, and a cysteine, after which the protein is categorized as a cysteine protease. Papain exhibits specific substrate preferences for hydrophobic or aromatic residues. | |||
== Secondary Structure == | == Secondary Structure == | ||
