1E8T

Structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

Summary for 1E8T

• Entry DOI: 10.2210/pdb1e8t/pdb
• Related: 1E8U 1E8V
• Descriptor: HEMAGGLUTININ-NEURAMINIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: sialidase, neuraminidase, hydrolase, hemagglutinin
• Biological source: Newcastle disease virus (strain Kansas)
• Total number of polymer chains: 2
• Total formula weight: 101100.19

Authors

Crennell, S.,Takimoto, T.,Portner, A.,Taylor, G. (deposition date: 2000-10-01, release date: 2001-04-03, Last modification date: 2024-11-06)

Primary citation

Crennell, S.,Takimoto, T.,Portner, A.,Taylor, G.
Crystal Structure of the Multifunctional Paramyxovirus Hemagglutinin-Neuraminidase
Nat.Struct.Biol., 7:1068-, 2000

PubMed Abstract: Paramyxoviruses are the main cause of respiratory disease in children. One of two viral surface glycoproteins, the hemagglutinin-neuraminidase (HN), has several functions in addition to being the major surface antigen that induces neutralizing antibodies. Here we present the crystal structures of Newcastle disease virus HN alone and in complex with either an inhibitor or with the beta-anomer of sialic acid. The inhibitor complex reveals a typical neuraminidase active site within a beta-propeller fold. Comparison of the structures of the two complexes reveal differences in the active site, suggesting that the catalytic site is activated by a conformational switch. This site may provide both sialic acid binding and hydrolysis functions since there is no evidence for a second sialic acid binding site in HN. Evidence for a single site with dual functions is examined and supported by mutagenesis studies. The structure provides the basis for the structure-based design of inhibitors for a range of paramyxovirus-induced diseases.

PubMed: 11062565
DOI: 10.1038/81002

Experimental method

X-RAY DIFFRACTION (2.5 Å)