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| | ==Zika virus capsid protein== | | ==Zika virus capsid protein== |
| - | <StructureSection load='6c44' size='340' side='right'caption='[[6c44]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6c44' size='340' side='right'caption='[[6c44]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c44]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Zikv Zikv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C44 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zika_virus Zika virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C44 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6c44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c44 OCA], [http://pdbe.org/6c44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c44 RCSB], [http://www.ebi.ac.uk/pdbsum/6c44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c44 ProSAT]</span></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6c44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c44 OCA], [https://pdbe.org/6c44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c44 RCSB], [https://www.ebi.ac.uk/pdbsum/6c44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c44 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1V0E2H9_ZIKV A0A1V0E2H9_ZIKV] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Virus coat protein|Virus coat protein]] | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Zikv]] | |
| - | [[Category: Almeida, F C.L]] | |
| - | [[Category: Barbosa, G M]] | |
| - | [[Category: Cruz-Oliveira, C]] | |
| - | [[Category: Morando, M A]] | |
| - | [[Category: Poian, A T.Da]] | |
| - | [[Category: Capsid]] | |
| - | [[Category: Rna binding protein]] | |
| - | [[Category: Viral protein]] | |
| | [[Category: Zika virus]] | | [[Category: Zika virus]] |
| | + | [[Category: Almeida FCL]] |
| | + | [[Category: Barbosa GM]] |
| | + | [[Category: Cruz-Oliveira C]] |
| | + | [[Category: Da Poian AT]] |
| | + | [[Category: Morando MA]] |
| Structural highlights
Function
A0A1V0E2H9_ZIKV
Publication Abstract from PubMed
Zika virus (ZIKV) became an important public health concern because infection was correlated to the development of microcephaly and other neurological disorders. Although the structure of the virion has been determined by cryo-electron microscopy, information about the nucleocapsid is lacking. We used nuclear magnetic resonance to determine the solution structure and dynamics of full length ZIKV capsid protein (ZIKVC). Although most of the protein is structured as described for the capsid proteins of Dengue and West Nile viruses and for truncated ZIKVC (residues 23-98), here we show important differences in the alpha-helix 1 and N-terminal intrinsically disordered region (IDR). We distinguished two dynamical regions in the ZIKVC IDR, a highly flexible N-terminal end and a transitional disordered region, indicating that it contains ordered segments rather than being completely flexible. The unique size and orientation of alpha-helix 1 partially occlude the protein hydrophobic cleft. Measurements of the dynamics of alpha-helix 1, surface exposure, and thermal susceptibility of each backbone amide (1)H in protein structure revealed the occlusion of the hydrophobic cleft by alpha1/alpha1' and supported alpha-helix 1 positional uncertainty. On the basis of the findings described here, we propose that the dynamics of ZIKVC structural elements responds to a structure-driven regulation of interaction of the protein with intracellular hydrophobic interfaces, which would have an impact on the switches that are necessary for nucleocapsid assembly. Subtle differences in the sequence of alpha-helix 1 have an impact on its size and orientation and on the degree of exposure of the hydrophobic cleft, suggesting that alpha-helix 1 is a hot spot for evolutionary adaptation of the capsid proteins of flaviviruses.
Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the alpha-Helix 1 Sequence.,Morando MA, Barbosa GM, Cruz-Oliveira C, Da Poian AT, Almeida FCL Biochemistry. 2019 May 21;58(20):2488-2498. doi: 10.1021/acs.biochem.9b00194., Epub 2019 May 6. PMID:31034208[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morando MA, Barbosa GM, Cruz-Oliveira C, Da Poian AT, Almeida FCL. Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the alpha-Helix 1 Sequence. Biochemistry. 2019 May 21;58(20):2488-2498. doi: 10.1021/acs.biochem.9b00194., Epub 2019 May 6. PMID:31034208 doi:http://dx.doi.org/10.1021/acs.biochem.9b00194
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