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4D1F

Crystal structure of the fiber head domain of the Atadenovirus snake adenovirus 1, native, first P212121 crystal form

Summary for 4D1F
Entry DOI10.2210/pdb4d1f/pdb
Related4D0U 4D0V 4D1G 4D1H
DescriptorFIBER PROTEIN, GLYCEROL (3 entities in total)
Functional Keywordsviral protein
Biological sourceSNAKE ADENOVIRUS 1
Cellular locationVirion : A9CB96
Total number of polymer chains12
Total formula weight184533.49
Authors
Singh, A.K.,van Raaij, M.J. (deposition date: 2014-05-01, release date: 2014-12-17, Last modification date: 2023-12-20)
Primary citationSingh, A.K.,Menendez-Conejero, R.,San Martin, C.,van Raaij, M.J.
Crystal structure of the fibre head domain of the Atadenovirus Snake Adenovirus 1.
PLoS ONE, 9:e114373-e114373, 2014
Cited by
PubMed Abstract: Adenoviruses are non-enveloped icosahedral viruses with trimeric fibre proteins protruding from their vertices. There are five known genera, from which only Mastadenoviruses have been widely studied. Apart from studying adenovirus as a biological model system and with a view to prevent or combat viral infection, there is a major interest in using adenovirus for vaccination, cancer therapy and gene therapy purposes. Adenoviruses from the Atadenovirus genus have been isolated from squamate reptile hosts, ruminants and birds and have a characteristic gene organization and capsid morphology. The carboxy-terminal virus-distal fibre head domains are likely responsible for primary receptor recognition. We determined the high-resolution crystal structure of the Snake Adenovirus 1 (SnAdV-1) fibre head using the multi-wavelength anomalous dispersion (MAD) method. Despite the absence of significant sequence homology, this Atadenovirus fibre head has the same beta-sandwich propeller topology as other adenovirus fibre heads. However, it is about half the size, mainly due to much shorter loops connecting the beta-strands. The detailed structure of the SnAdV-1 fibre head and other animal adenovirus fibre heads, together with the future identification of their natural receptors, may lead to the development of new strategies to target adenovirus vectors to cells of interest.
PubMed: 25486282
DOI: 10.1371/journal.pone.0114373
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

229380

數據於2024-12-25公開中

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