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GP1 of Lassa Virus

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Attached to this structure is a unique <scene name='76/761695/Histriad/5'>triad of histidines</scene> that is highly conserved among Old World arenaviruses. Located on the β-sheet face of GP1, the histidine triad is a structural element that directly interacts with [[LAMP1]] (Lysosome-associated membrane glycoprotein) and helps stabilize a LAMP1-"compatible" conformation by providing a molecular mechanism for the pH-dependent receptor switching<ref name="MolMechforLAMP1" />. The histidine triad is critical in forming a binding site for LAMP1 (insert scene).
Attached to this structure is a unique <scene name='76/761695/Histriad/5'>triad of histidines</scene> that is highly conserved among Old World arenaviruses. Located on the β-sheet face of GP1, the histidine triad is a structural element that directly interacts with [[LAMP1]] (Lysosome-associated membrane glycoprotein) and helps stabilize a LAMP1-"compatible" conformation by providing a molecular mechanism for the pH-dependent receptor switching<ref name="MolMechforLAMP1" />. The histidine triad is critical in forming a binding site for LAMP1 (insert scene).
===LAMP1 Binding Site===
===LAMP1 Binding Site===
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The primary cellular receptor of LASV is α-dystroglycan (α-DG)<ref>DOI 10.1128/JVI.00651-15</ref>
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The primary cellular receptor of LASV is α-dystroglycan (α-DG)

Revision as of 10:59, 27 June 2017

4ZJF structure

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 Cohen-Dvashi H, Cohen N, Israeli H, Diskin R. Molecular mechanism for LAMP1 recognition by Lassa Virus. J Virol. 2015 May 13. pii: JVI.00651-15. PMID:25972533 doi:http://dx.doi.org/10.1128/JVI.00651-15

Proteopedia Page Contributors and Editors (what is this?)

Rebecca Holstein, Michal Harel

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