6c44

Zika virus capsid proteinZika virus capsid protein

Structural highlights 6c44 is a 2 chain structure with sequence from Zika virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

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