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5c02

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Revision as of 11:08, 25 December 2019

Influenza A M2 transmembrane domain drug-resistant S31N mutant at pH 8.0

Structural highlights

5c02 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
NonStd Res:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[M2_I03A0] Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation (By similarity).

Publication Abstract from PubMed

The M2 protein is a small proton channel found in the influenza A virus that is necessary for viral replication. The M2 channel is the target of a class of drugs called the adamantanes, which block the channel pore and prevent the virus from replicating. In recent decades mutations have arisen in M2 that prevent the adamantanes from binding to the channel pore, with the most prevalent of these mutations being S31N. Here we report the first crystal structure of the S31N mutant crystallized using lipidic cubic phase crystallization techniques and solved to 1.59 A resolution. The Asn31 residues point directly into the center of the channel pore and form a hydrogen-bonded network that disrupts the drug-binding site. Ordered waters in the channel pore form a continuous hydrogen bonding network from Gly34 to His37. This article is protected by copyright. All rights reserved.

Crystal structure of the drug-resistant S31N influenza M2 proton channel.,Thomaston JL, DeGrado WF Protein Sci. 2016 Apr 15. doi: 10.1002/pro.2937. PMID:27082171^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Thomaston JL, DeGrado WF. Crystal structure of the drug-resistant S31N influenza M2 proton channel. Protein Sci. 2016 Apr 15. doi: 10.1002/pro.2937. PMID:27082171 doi:http://dx.doi.org/10.1002/pro.2937

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5c02"

@@ Line 1: / Line 1: @@
 ==Influenza A M2 transmembrane domain drug-resistant S31N mutant at pH 8.0==
-<StructureSection load='5c02' size='340' side='right' caption='[[5c02]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
+<StructureSection load='5c02' size='340' side='right'caption='[[5c02]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5c02]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C02 FirstGlance]. <br>
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5c02" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ion channels 3D structures|Ion channels 3D structures]]
+*[[M2 protein|M2 protein]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: DeGrado, W F]]
 [[Category: Thomaston, J L]]

5c02

From Proteopedia

Revision as of 11:08, 25 December 2019

Influenza A M2 transmembrane domain drug-resistant S31N mutant at pH 8.0

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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