Proteopedia:Featured SEL/0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: <table> <tr><td>Image:Oct2017.png</td></tr> <tr><td>'''HIV-1 protease'''</td></tr> <tr><td>''David Canner''</td></tr> <tr><td>The X-ray structure of HIV-1 protease reveals that it is c...)
Current revision (12:01, 19 October 2018) (edit) (undo)
(image must be a link)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
<table>
<table>
-
<tr><td>[[Image:Oct2017.png]]</td></tr>
+
<tr><td>
-
<tr><td>'''HIV-1 protease'''</td></tr>
+
<imagemap>
-
<tr><td>''David Canner''</td></tr>
+
Image:Anim HIV protease.gif|center
-
<tr><td>The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits, each consisting of 99 amino acid residues. The subunits come together in such as way as to form a tunnel where they meet. This tunnel is of critical importance because the active site of the protease is located in its interior. The active site consists of two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two Asp's are essential catalytic residues either interact with the incoming water OR protonate the carbonyl to make the carbon more electrophilic for the incoming water.</td></tr>
+
default [[Immunodeficiency virus protease]]
 +
</imagemap>
 +
</td></tr>
 +
<tr><td><div class='scrolling '>'''HIV-1 protease'''<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.
 +
 
 +
>>> [[Immunodeficiency virus protease|Visit this page]] >>>
 +
</div>
 +
</td></tr>
</table>
</table>
 +
 +
[[Category:Featured in Selected Pages]]

Current revision

About this image
HIV-1 protease

by David Canner
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.

>>> Visit this page >>>

Proteopedia Page Contributors and Editors (what is this?)

Angel Herraez, Jaime Prilusky

Retrieved from "http://52.214.119.220/wiki/index.php/Proteopedia:Featured_SEL/0"
Personal tools