3c9j: Difference between revisions

Revision as of 20:14, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3c9j.png

Template:STRUCTURE 3c9j

The Crystal structure of Transmembrane domain of M2 protein and Amantadine complexThe Crystal structure of Transmembrane domain of M2 protein and Amantadine complex

Template:ABSTRACT PUBMED 18235504

About this StructureAbout this Structure

3C9J is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the function and inhibition of an influenza virus proton channel., Stouffer AL, Acharya R, Salom D, Levine AS, Di Costanzo L, Soto CS, Tereshko V, Nanda V, Stayrook S, DeGrado WF, Nature. 2008 Jan 31;451(7178):596-9. PMID:18235504

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OCA

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-'''The Crystal structure of Transmembrane domain of M2 protein and Amantadine complex'''
+===The Crystal structure of Transmembrane domain of M2 protein and Amantadine complex===
-==Overview==
+<!--
-The M2 protein from influenza A virus is a pH-activated proton channel that mediates acidification of the interior of viral particles entrapped in endosomes. M2 is the target of the anti-influenza drugs amantadine and rimantadine; recently, resistance to these drugs in humans, birds and pigs has reached more than 90% (ref. 1). Here we describe the crystal structure of the transmembrane-spanning region of the homotetrameric protein in the presence and absence of the channel-blocking drug amantadine. pH-dependent structural changes occur near a set of conserved His and Trp residues that are involved in proton gating. The drug-binding site is lined by residues that are mutated in amantadine-resistant viruses. Binding of amantadine physically occludes the pore, and might also perturb the pK(a) of the critical His residue. The structure provides a starting point for solving the problem of resistance to M2-channel blockers.
+The line below this paragraph, {{ABSTRACT_PUBMED_18235504}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18235504 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18235504}}
 ==About this Structure==
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 [[Category: Membrane protein]]
 [[Category: Proton channel]]
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