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2WSU

Galectin domain of porcine adenovirus type 4 NADC-1 isolate fibre

Summary for 2WSU
Entry DOI10.2210/pdb2wsu/pdb
Related2WST 2WSV 2WT0 2WT1 2WT2
DescriptorPUTATIVE FIBER PROTEIN, GLYCEROL, NITRATE ION, ... (4 entities in total)
Functional Keywordsviral protein, carbohydrate recognition domain, tandem-repeat-type
Biological sourcePORCINE ADENOVIRUS 4
Total number of polymer chains4
Total formula weight152933.25
Authors
Guardado-Calvo, P.,Munoz, E.M.,Llamas-Saiz, A.L.,Fox, G.C.,Glasgow, J.N.,van Raaij, M.J. (deposition date: 2009-09-10, release date: 2010-08-11, Last modification date: 2023-12-20)
Primary citationGuardado-Calvo, P.,Munoz, E.M.,Llamas-Saiz, A.L.,Fox, G.C.,Kahn, R.,Curiel, D.T.,Glasgow, J.N.,van Raaij, M.J.
Crystallographic structure of porcine adenovirus type 4 fiber head and galectin domains.
J. Virol., 84:10558-10568, 2010
Cited by
PubMed Abstract: Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N-acetyl-lactosamine units, and we present structures of the galectin domain with lactose, N-acetyl-lactosamine, 3-aminopropyl-lacto-N-neotetraose, and 2-aminoethyl-tri(N-acetyl-lactosamine), confirming the domain as a bona fide galectin domain.
PubMed: 20686025
DOI: 10.1128/JVI.00997-10
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2024-11-06公开中

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