2WSU
Galectin domain of porcine adenovirus type 4 NADC-1 isolate fibre
Summary for 2WSU
Entry DOI | 10.2210/pdb2wsu/pdb |
Related | 2WST 2WSV 2WT0 2WT1 2WT2 |
Descriptor | PUTATIVE FIBER PROTEIN, GLYCEROL, NITRATE ION, ... (4 entities in total) |
Functional Keywords | viral protein, carbohydrate recognition domain, tandem-repeat-type |
Biological source | PORCINE ADENOVIRUS 4 |
Total number of polymer chains | 4 |
Total formula weight | 152933.25 |
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 citation | Guardado-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: 20686025DOI: 10.1128/JVI.00997-10 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report