 |
PDBsum entry 4jf7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
4jf7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Viral protein
|
|
|
Title:
|
|
Structure of the parainfluenza virus 5 (piv5) hemagglutinin- neuraminidase (hn) ectodomain
|
|
Structure:
|
|
Hemagglutinin-neuraminidase. Chain: d, a, b, c. Fragment: ectodomain. Engineered: yes
|
|
Source:
|
|
Simian virus 5. Sv5. Organism_taxid: 11208. Strain: w3. Gene: hn. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.
|
|
Resolution:
|
|
|
2.50Å
|
R-factor:
|
0.166
|
R-free:
|
0.207
|
|
|
Authors:
|
|
B.D.Welch,P.Yuan,S.Bose,C.A.Kors,R.A.Lamb,T.S.Jardetzky
|
|
Key ref:
|
|
B.D.Welch
et al.
(2013).
Structure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomain.
Plos Pathog,
9,
e1003534.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
27-Feb-13
|
Release date:
|
04-Sep-13
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P04850
(HN_PIV5) -
Hemagglutinin-neuraminidase from Parainfluenza virus 5 (strain W3)
|
|
|
|
Seq:
Struc:
|
|
|
|
565 a.a.
492 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.2.1.18
- exo-alpha-sialidase.
|
|
|
|
|
|
|
Reaction:
|
|
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Plos Pathog
9:e1003534
(2013)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomain.
|
|
B.D.Welch,
P.Yuan,
S.Bose,
C.A.Kors,
R.A.Lamb,
T.S.Jardetzky.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Paramyxoviruses cause a wide variety of human and animal diseases. They infect
host cells using the coordinated action of two surface glycoproteins, the
receptor binding protein (HN, H, or G) and the fusion protein (F). HN binds
sialic acid on host cells (hemagglutinin activity) and hydrolyzes these
receptors during viral egress (neuraminidase activity, NA). Additionally,
receptor binding is thought to induce a conformational change in HN that
subsequently triggers major refolding in homotypic F, resulting in fusion of
virus and target cell membranes. HN is an oligomeric type II transmembrane
protein with a short cytoplasmic domain and a large ectodomain comprising a long
helical stalk and large globular head domain containing the enzymatic functions
(NA domain). Extensive biochemical characterization has revealed that HN-stalk
residues determine F specificity and activation. However, the F/HN interaction
and the mechanisms whereby receptor binding regulates F activation are poorly
defined. Recently, a structure of Newcastle disease virus (NDV) HN ectodomain
revealed the heads (NA domains) in a "4-heads-down" conformation
whereby two of the heads form a symmetrical interaction with two sides of the
stalk. The interface includes stalk residues implicated in triggering F, and the
heads sterically shield these residues from interaction with F (at least on two
sides). Here we report the x-ray crystal structure of parainfluenza virus 5
(PIV5) HN ectodomain in a "2-heads-up/2-heads-down" conformation where
two heads (covalent dimers) are in the "down position," forming a
similar interface as observed in the NDV HN ectodomain structure, and two heads
are in an "up position." The structure supports a model in which the
heads of HN transition from down to up upon receptor binding thereby releasing
steric constraints and facilitating the interaction between critical HN-stalk
residues and F.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
