PDBsum entry 4gjt

Membrane protein/viral protein

PDB id: 4gjt

Contents

Protein chains

411 a.a.

114 a.a.

Ligands

NAG

Waters ×79

PDB id:

4gjt

Name:

Membrane protein/viral protein

Title:

Complex structure of nectin-4 bound to mv-h

Structure:

Hemagglutinin glycoprotein. Chain: a. Fragment: mv-h fragment, 156-617. Engineered: yes. Poliovirus receptor-related protein 4. Chain: b, c. Fragment: nectin-4 fragment, 32-145. Synonym: ig superfamily receptor lnir, nectin-4, processed poliovirus receptor-related protein 4.

Source:

Measles virus. Mev. Organism_taxid: 645098. Strain: ichinose-b95a. Gene: h, hemagglutinin. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: hifive insect cells. Homo sapiens.

Resolution:

3.10Å R-factor: 0.261 R-free: 0.278

Authors:

X.Zhang,G.Lu,J.Qi,Y.Li,Y.He,X.Xu,J.Shi,C.Zhang,J.Yan,G.F.Gao

Key ref:

X.Zhang et al. (2013). Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4. Nat Struct Biol, 20, 67-72. PubMed id: 23202587

Date:

10-Aug-12 Release date: 10-Oct-12

Protein chain

Q786F2  (HEMA_MEASC) -  Hemagglutinin glycoprotein from Measles virus (strain Ichinose-B95a)

Seq: 617 a.a.

Struc: 411 a.a.

Protein chains

Q96NY8  (NECT4_HUMAN) -  Nectin-4 from Homo sapiens

Seq: 510 a.a.

Struc: 114 a.a.

Nat Struct Biol 20:67-72 (2013)

PubMed id: 23202587

Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.

X.Zhang, G.Lu, J.Qi, Y.Li, Y.He, X.Xu, J.Shi, C.W.Zhang, J.Yan, G.F.Gao.

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.