User:Eric Martz/Sandbox 8

spinqualitylabelsall models Influenza Neuraminidase N1 (2hu4). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Neuraminidase Structure and Conserved Amino AcidsNeuraminidase Structure and Conserved Amino Acids

• Influenza neuraminidase is a homotetramer ().

• Each of the four protein chains in the tetramer has a catalytic site, indicated in by the positions of the bound Tamiflu inhibitors.

• The involves only a single protein chain, being distant from neighboring chains.

• The is mostly beta, consisting of several beta sheets with three short alpha helices ( Beta Strands , Alpha Helices).

• The residues contacting the Tamiflu inhibitory substrate analog are .

• These highly conserved residues include some known to be crucial to binding sialic acid substrate: Arg 118, Arg 292 and Arg 371 bind the carboxylate; Arg 152 interacts with the acetamido substituent; and Glu 276 forms hydrogen bonds with the 8- and 9-hydroxyl groups of the substrate. These residues are in contact with the sialic acid substrate analog Tamiflu. In this scene, atoms and bonds in Tamiflu and the highlighted residues are colored by element: C, O, N.