This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
GP1 of Lassa Virus
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
'''GP1''' (Glycoprotein 1) is the receptor binding domain of Lassa virus that mediates receptor recognition. Research thus far indicates that GP1 from Lassa virus may undergo irreversible conformational changes that could serve as an immunological decoy mechanism. | '''GP1''' (Glycoprotein 1) is the receptor binding domain of Lassa virus that mediates receptor recognition. Research thus far indicates that GP1 from Lassa virus may undergo irreversible conformational changes that could serve as an immunological decoy mechanism. | ||
==Structural Highlights== | ==Structural Highlights== | ||
| - | Protein structure accession number: '''4ZJF'''. 4ZJF is a 4 chain structure with <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> ligands attached to each chain. The overall architecture of GP1 features a central β-sheet and two distinct halves: a glycosylated half containing the receptor-binding site that is made mostly by the central β-sheet and surrounding loops and a half that contains mostly helices and most likely faces the trimer axis<ref name="MolMechforLAMP1">DOI 10.1128/JVI.00651-15</ref>. The method to determine this structure was | + | Protein structure accession number: '''4ZJF'''. 4ZJF is a 4 chain structure with <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> ligands attached to each chain. The overall architecture of GP1 features a central β-sheet and two distinct halves: a glycosylated half containing the receptor-binding site that is made mostly by the central β-sheet and surrounding loops and a half that contains mostly helices and most likely faces the trimer axis<ref name="MolMechforLAMP1">DOI 10.1128/JVI.00651-15</ref>. The method used to determine this structure was |
[https://en.wikipedia.org/wiki/X-ray_crystallography X-ray diffraction] | [https://en.wikipedia.org/wiki/X-ray_crystallography X-ray diffraction] | ||
=== Histidine Triad=== | === Histidine Triad=== | ||
Revision as of 08:59, 26 June 2017
| |||||||||||
References
- ↑ 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
Categories: Cohen, N | Cohen-Dvashi, H | Diskin, R | Israeli, H | Arenaviruse | Glycoprotein | Lassa | Receptor binding | Viral protein | 4zjf
