3IXT

Crystal Structure of Motavizumab Fab Bound to Peptide Epitope

Summary for 3IXT

• Entry DOI: 10.2210/pdb3ixt/pdb
• Descriptor: Motavizumab Fab light chain, Motavizumab Fab heavy chain, Fusion glycoprotein F1, ... (5 entities in total)
• Functional Keywords: fab, rsv, synagis, motavizumab, monoclonal, complex, cell membrane, cleavage on pair of basic residues, disulfide bond, envelope protein, fusion protein, glycoprotein, lipoprotein, membrane, palmitate, transmembrane, virion, immune system
• Biological source: Mus musculus (mouse); More
• Cellular location: Virion membrane; Single-pass type I membrane protein: P03420
• Total number of polymer chains: 6
• Total formula weight: 100574.88

Authors

McLellan, J.S.,Chen, M.,Kim, A.,Yang, Y.,Graham, B.S.,Kwong, P.D. (deposition date: 2009-09-04, release date: 2010-01-19, Last modification date: 2024-11-27)

Primary citation

McLellan, J.S.,Chen, M.,Kim, A.,Yang, Y.,Graham, B.S.,Kwong, P.D.
Structural basis of respiratory syncytial virus neutralization by motavizumab.
Nat.Struct.Mol.Biol., 17:248-250, 2010

PubMed Abstract: Motavizumab is approximately tenfold more potent than its predecessor, palivizumab (Synagis), the FDA-approved monoclonal antibody used to prevent respiratory syncytial virus (RSV) infection. The structure of motavizumab in complex with a 24-residue peptide corresponding to its epitope on the RSV fusion (F) glycoprotein reveals the structural basis for this greater potency. Modeling suggests that motavizumab recognizes a different quaternary configuration of the F glycoprotein than that observed in a homologous structure.

PubMed: 20098425
DOI: 10.1038/nsmb.1723

Experimental method

X-RAY DIFFRACTION (2.75 Å)