Sandbox Reserved 1056: Difference between revisions
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== | ==Carboxypeptidase A in ''B. taurus''== | ||
<StructureSection load=' | <StructureSection load='1cpx' size='340' side='right' caption='Caption for this structure' scene=''> | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
===Introduction=== | |||
== Biological Function == | == Biological Function == | ||
== Structural Overview == | == Structural Overview == | ||
== Structural highlights == | |||
[[Image:Hydrophobic_C-terminal_Side_Chain_Binding_Site_with_Y248.png|200 px|left|thumb|Carboxypeptidase A in ''B. taurus.'' The red highlights the hydrophobic binding pocket while the blue highlights Y248.]] | |||
Shown to the left is the hydrophobic binding pocket of Carboxypeptidase A in ''B. taurus'' in relation to the whole molecule. It is one of the molecule's most important structural features. The <scene name='69/694223/Hydrophobic_binding_pocket_2/2'>hydrophobic binding pocket</scene> is also isolated in the 3D applet to the right. This binding pocket is the site at which C-terminal side chain of the substrate binds. It is formed by amino acid residues I243, I247, A250, G252, G253, S254 and I255. | |||
Nearby, there is also Y198 which serves as the recognition site for the sidechain next to the C-terminal residue. | |||
== Mechanism of Action == | == Mechanism of Action == | ||