4GJT

complex structure of nectin-4 bound to MV-H

Summary for 4GJT

• Entry DOI: 10.2210/pdb4gjt/pdb
• Related: 2RKC 2ZB5 3ALW 3INB
• Descriptor: Hemagglutinin glycoprotein, Poliovirus receptor-related protein 4, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: six-bladed -propeller, igv-like fold, viral entry, mv-h, nectin-4, beta4/beta5 groove, membrane protein-viral protein complex, membrane protein/viral protein
• Biological source: Measles virus (MeV); More
• Total number of polymer chains: 3
• Total formula weight: 79870.10

Authors

Zhang, X.,Lu, G.,Qi, J.,Li, Y.,He, Y.,Xu, X.,Shi, J.,Zhang, C.,Yan, J.,Gao, G.F. (deposition date: 2012-08-10, release date: 2012-10-10, Last modification date: 2024-10-30)

Primary citation

Zhang, X.,Lu, G.,Qi, J.,Li, Y.,He, Y.,Xu, X.,Shi, J.,Zhang, C.W.,Yan, J.,Gao, G.F.
Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4
Nat.Struct.Mol.Biol., 20:67-72, 2013

PubMed Abstract: Measles virus is a major public health concern worldwide. Three measles virus cell receptors have been identified so far, and the structures of the first two in complex with measles virus hemagglutinin (MV-H) have been reported. Nectin-4 is the most recently identified receptor in epithelial cells, and its binding mode to MV-H remains elusive. In this study, we solved the structure of the membrane-distal domain of human nectin-4 in complex with MV-H. The structure shows that nectin-4 binds the MV-H β4-β5 groove exclusively via its N-terminal IgV domain; the contact interface is dominated by hydrophobic interactions. The binding site in MV-H for nectin-4 also overlaps extensively with those of the other two receptors. Finally, a hydrophobic pocket centered in the β4-β5 groove is involved in binding to all three identified measles virus receptors, representing a potential target for antiviral drugs.

PubMed: 23202587
DOI: 10.1038/nsmb.2432

Experimental method

X-RAY DIFFRACTION (3.1001 Å)