ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization of the head and galectin-like domains of porcine adenovirus isolate NADC-1 fibre.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Characterization of the First Genome of Porcine mastadenovirus B (HNU1 Strain) and Implications on Its Lymphoid and Special Origin.Virologica Sinica · 2020Article
- An adenovirus vector incorporating carbohydrate binding domains utilizes glycans for gene transfer.PloS one · 2013Article
- Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Crystallographic structure of porcine adenovirus type 4 fiber head and galectin domains.Journal of virology · 2010Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The porcine adenovirus NADC-1 isolate, a strain of porcine adenovirus type 4, has a fibre with an atypical architecture. In addition to a classical virus attachment region, shaft and head domains, it contains an additional galectin like domain C-terminal to the head domain and connected to the head domain by a long RGD-containing loop. The galectin-like domain contains two putative carbohydrate-recognition domains. The head and galectin-like domains have been independently crystallized. Diffraction data have been obtained to 3.2 angstrom resolution from crystals of the head domain and to 1.9 angstrom resolution from galectin-like domain crystals.
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