We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5gs6

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Full-length NS1 structure of Zika virus from 2015 Brazil strain

Structural highlights

5gs6 is a 2 chain structure with sequence from Zika virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.852Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A109PRQ3_ZIKV Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504]

Publication Abstract from PubMed

The association of Zika virus (ZIKV) infections with microcephaly and neurological diseases has highlighted an emerging public health concern. Here, we report the crystal structure of the full-length ZIKV nonstructural protein 1 (NS1), a major host-interaction molecule that functions in flaviviral replication, pathogenesis, and immune evasion. Of note, a long intertwined loop is observed in the wing domain of ZIKV NS1, and forms a hydrophobic "spike", which can contribute to cellular membrane association. For different flaviviruses, the amino acid sequences of the "spike" are variable but their common characteristic is either hydrophobic or positively charged, which is a beneficial feature for membrane binding. Comparative studies with West Nile and Dengue virus NS1 structures reveal conserved features, but diversified electrostatic characteristics on both inner and outer faces. Our results suggest different mechanisms of flavivirus pathogenesis and should be considered during the development of diagnostic tools.

Contribution of intertwined loop to membrane association revealed by Zika virus full-length NS1 structure.,Xu X, Song H, Qi J, Liu Y, Wang H, Su C, Shi Y, Gao GF EMBO J. 2016 Aug 30. pii: e201695290. PMID:27578809^[1]

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

References

↑ Xu X, Song H, Qi J, Liu Y, Wang H, Su C, Shi Y, Gao GF. Contribution of intertwined loop to membrane association revealed by Zika virus full-length NS1 structure. EMBO J. 2016 Aug 30. pii: e201695290. PMID:27578809 doi:http://dx.doi.org/10.15252/embj.201695290

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gs6"

@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/A0A109PRQ3_ZIKV A0A109PRQ3_ZIKV] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504]  Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]
+[https://www.uniprot.org/uniprot/A0A109PRQ3_ZIKV A0A109PRQ3_ZIKV] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

5gs6

From Proteopedia

Current revision

Full-length NS1 structure of Zika virus from 2015 Brazil strain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox