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2gg1

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Revision as of 06:46, 19 February 2020

NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)

Structural highlights

2gg1 is a 1 chain structure with sequence from Flavivirus langat. This structure supersedes the now removed PDB entry 1yzo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1z66
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POLG_LANVY] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Flaviviruses cause many human diseases, including dengue fever, yellow fever, West Nile viral encephalitis, and hemorrhagic fevers, and are transmitted to their vertebrate hosts by infected mosquitoes and ticks. Domain III of the envelope protein (E-D3) is considered to be the primary viral determinant involved in the virus-host-cell receptor interaction, and thus represents an excellent target for antiviral drug development. Langat (LGT) virus is a naturally attenuated BSL-2 TBE virus and is a model for the pathogenic BSL-3 and BSL-4 viruses in the serogroup. We have determined the solution structure of LGT-E-D3 using heteronuclear NMR spectroscopy. The backbone dynamics of LGT-E-D3 have been investigated using 15N relaxation measurements. A detailed analysis of the solution structure and dynamics of LGT-E-D3 suggests potential residues that could form a surface for molecular recognition, and thereby represent a target site for antiviral therapeutics design.

NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition.,Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO Protein Sci. 2006 Jun;15(6):1342-55. PMID:16731969^[1]

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

References

↑ Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO. NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition. Protein Sci. 2006 Jun;15(6):1342-55. PMID:16731969 doi:15/6/1342

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gg1"

@@ Line 1: / Line 1: @@
 ==NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)==
-<StructureSection load='2gg1' size='340' side='right' caption='[[2gg1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2gg1' size='340' side='right'caption='[[2gg1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2gg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavivirus_langat Flavivirus langat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yzo 1yzo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GG1 FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Flavivirus langat]]
+[[Category: Large Structures]]
 [[Category: Cowburn, D]]
 [[Category: Dutta, K]]

2gg1

From Proteopedia

Revision as of 06:46, 19 February 2020

NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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