Proteopedia:Featured SEL/0: Difference between revisions
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<tr><td><div class='scrolling '>'''HIV-1 protease'''<br> | <tr><td><div class='scrolling '>'''HIV-1 protease'''<br> | ||
''David Canner''<br> | ''by David Canner''<br> | ||
The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits which form a tunnel where they meet. This is critical because it contains the active site of the protease, consisting on two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two catalytic Asp's either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water. | The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits which form a tunnel where they meet. This is critical because it contains the active site of the protease, consisting on two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two catalytic Asp's either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water. | ||
Latest revision as of 15:01, 19 October 2018
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HIV-1 protease
by David Canner >>> Visit this page >>> |