PDBsum entry 4zcj

Viral protein

PDB id: 4zcj

Contents

Protein chains

316 a.a.

172 a.a.

Ligands

NAG-NAG-BMA

NAG-NAG

NAG ×5

PDB id:

4zcj

Name:

Viral protein

Title:

Crystal structure of the a/hong kong/1/1968 (h3n2) influenza virus hemagglutinin ha1 cys30, ha2 cys47 mutant

Structure:

Hemagglutinin. Chain: a, c, e. Fragment: ha1 chain (unp residues 27-345). Engineered: yes. Hemagglutinin. Chain: b, d, f. Fragment: ha2 chain (unp residues 346-521). Engineered: yes

Source:

Influenza a virus (strain a/hong kong/1/1968 h3n2). Organism_taxid: 506350. Strain: a/hong kong/1/1968 h3n2. Gene: ha. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_taxid: 7111

Resolution:

3.00Å R-factor: 0.249 R-free: 0.275

Authors:

P.S.Lee,I.A.Wilson

Key ref:

P.S.Lee et al. (2015). Design and Structure of an Engineered Disulfide-Stabilized Influenza Virus Hemagglutinin Trimer. J Virol, 89, 7417-7420. PubMed id: 25926650 DOI: 10.1128/JVI.00808-15

Date:

16-Apr-15 Release date: 13-May-15

Protein chains

Q91MA7  (HEMA_I68A4) -  Hemagglutinin from Influenza A virus (strain A/Hong Kong/1/1968 H3N2)

Seq: 566 a.a.

Struc: 316 a.a.*

Protein chains

Q91MA7  (HEMA_I68A4) -  Hemagglutinin from Influenza A virus (strain A/Hong Kong/1/1968 H3N2)

Seq: 566 a.a.

Struc: 172 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

DOI no: 10.1128/JVI.00808-15

J Virol 89:7417-7420 (2015)

PubMed id: 25926650

Design and Structure of an Engineered Disulfide-Stabilized Influenza Virus Hemagglutinin Trimer.

P.S.Lee, X.Zhu, W.Yu, I.A.Wilson.

ABSTRACT

We engineered a disulfide-stabilized influenza virus hemagglutinin (HA) trimer, termed HA3-SS, by introducing cysteine residues into the HA stem to covalently bridge the three protomers. HA3-SS has increased thermostability compared to wild-type HA, and binding of head- and stem-targeted antibodies (Abs) is preserved; only minor structural changes are found in the vicinity of the additional disulfide. This platform has been applied to H1 and H3 HAs and provides prospects for design of intact, stabilized influenza virus HA immunogens.