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| http://purl.uniprot.org/citations/30121295 | http://www.w3.org/2000/01/rdf-schema#comment | "We report the revised crystal structure of a pseudo-typed human adenovirus at 3.8-Å resolution that is consistent with the atomic models of minor proteins determined by cryo-electron microscopy. The diffraction data from multiple crystals were rescaled and merged to increase the data completeness. The densities for the minor proteins were initially identified in the phase-refined omit maps that were further improved by the phases from docked poly-alanine models to build atomic structures. While the trimeric fiber molecules are disordered due to flexibility and imposition of 5-fold symmetry, the remaining major capsid proteins hexon and penton base are clearly ordered, with the exception of hypervariable region 1 of hexons, the RGD containing loop, and the N-termini of the penton base. The exterior minor protein IX together with the interior minor proteins IIIa and VIII stabilizes the adenovirus virion. A segment of N-terminal pro-peptide of VI is found in the interior cavities of peripentonal hexons, and the rest of VI is disordered. While the triskelion substructures formed by the N-termini of IX conform to excellent quasi 3-fold symmetry, the tetrameric coiled-coils formed by the C-termini and organized in parallel and anti-parallel arrangement do not exhibit any quasi-symmetry. This observation also conveys the pitfalls of using the quasi-equivalence as validation criteria for the structural analysis of extended (non-modular) capsid proteins such as IX. Together, these results remedy certain discrepancies in the previous X-ray model in agreement with the cryo-electron microscopy models."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2018.08.011"xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/author | "Nemerow G.R."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/author | "Reddy V.S."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/author | "Venkataraman S."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/author | "Mullen T.M."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/author | "Kundhavai Natchiar S."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/pages | "4132-4141"xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/title | "Revised Crystal Structure of Human Adenovirus Reveals the Limits on Protein IX Quasi-Equivalence and on Analyzing Large Macromolecular Complexes."xsd:string |
| http://purl.uniprot.org/citations/30121295 | http://purl.uniprot.org/core/volume | "430"xsd:string |
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