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PDBsum entry 3inb

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protein ligands Protein-protein interface(s) links
Viral protein/immune system PDB id
3inb
Jmol
Contents
Protein chains
389 a.a.
126 a.a. *
Ligands
NAG ×6
SO4 ×3
Waters ×8
* Residue conservation analysis
PDB id:
3inb
Name: Viral protein/immune system
Title: Structure of the measles virus hemagglutinin bound to the cd receptor
Structure: Hemagglutinin glycoprotein. Chain: a, b. Fragment: head domain, residues 179-617. Engineered: yes. Membrane cofactor protein. Chain: c, d. Fragment: sushi domains 1 and 2, residues 35-160. Synonym: trophoblast leukocyte common antigen, tlx. Engineered: yes
Source: Measles virus strain edmonston. Viruses. Organism_taxid: 11235. Strain: edmonston. Gene: h. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: ovary cells. Homo sapiens.
Resolution:
3.10Å     R-factor:   0.228     R-free:   0.259
Authors: C.Santiago,M.L.Celma,T.Stehle,J.M.Casasnovas
Key ref:
C.Santiago et al. (2010). Structure of the measles virus hemagglutinin bound to the CD46 receptor. Nat Struct Biol, 17, 124-129. PubMed id: 20010840 DOI: 10.1038/nsmb.1726
Date:
12-Aug-09     Release date:   22-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08362  (HEMA_MEASE) -  Hemagglutinin glycoprotein
Seq:
Struc:
 
Seq:
Struc:
617 a.a.
389 a.a.*
Protein chains
Pfam   ArchSchema ?
P15529  (MCP_HUMAN) -  Membrane cofactor protein
Seq:
Struc:
392 a.a.
126 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     viral envelope   1 term 
  Biological process     viral infectious cycle   1 term 
  Biochemical function     host cell surface receptor binding     2 terms  

 

 
DOI no: 10.1038/nsmb.1726 Nat Struct Biol 17:124-129 (2010)
PubMed id: 20010840  
 
 
Structure of the measles virus hemagglutinin bound to the CD46 receptor.
C.Santiago, M.L.Celma, T.Stehle, J.M.Casasnovas.
 
  ABSTRACT  
 
The highly contagious measles virus infects millions of individuals worldwide, causing serious disease in children of developing countries. Infection is initiated by attachment of the measles virus hemagglutinin (MV-H), a glycoprotein anchored to the virus envelope, to the host cell receptors CD46 or signaling lymphocyte activation molecule (SLAM). Here we report the crystal structure of MV-H in complex with a CD46 protein spanning the two N-terminal domains. A unique groove at the side of the MV-H beta-propeller domain, which is absent in homologous paramyxovirus attachment proteins, engages residues in both CD46 domains. Key contacts involve a protruding loop in the N-terminal CD46 domain that carries two sequential proline residues (PP motif) and penetrates deeply into a hydrophobic socket in MV-H. We identify a similar PP motif in SLAM, defining a common measles virus recognition epitope in the CD46 and SLAM receptor proteins.
 
  Selected figure(s)  
 
Figure 1.
(a) Representation of the dimeric MV-H–CD46 complex present in the asymmetric unit of the crystals. Ribbon drawings of the MV-H molecules are shown with a rainbow coloring scheme, whereas Cα traces of the CD46 molecules are shown in blue. The six β-sheets building the MV-H β-propeller domain are labeled. The C-terminal residues of the molecules, shown as spheres, are followed by a polypeptide stalk in the full-length MV-H protein or the SCR3 and SCR4 domains in the CD46 molecule. Putative location of the virus and cell membranes are shown. (b) Detailed view of the MV-H–CD46 interface. Two side views, differing by 120°, are shown. CD46 residues buried by the interaction with MV-H are shown with spheres colored in dark blue (contact region 1, the D′D loop of SCR1), magenta (contact region 2, the SCR1-SCR2 interdomain region) and light blue (contact region 3, residues at SCR2).
Figure 2.
Ribbon drawing of the three MV-H–CD46 interacting regions described in Figure 1b. CD46 and MV-H are shown in blue and orange, respectively. Buried residues participating in critical contacts are depicted in stick representation and labeled in the three panels, with oxygens and nitrogens shown in red and blue, respectively. Side chains of MV-H residues engaged in hydrogen bonds (black dashed lines) with CD46 are highlighted in magenta, whereas cysteines are yellow. (a) Contact region 1, showing relevant contacts between MV-H and CD46 residues at the D′D loop of SCR1 (Ile37–Leu40). Loops connecting the β-strands s2 and s3 (s2-s3) of blade β4 and the blades β4 and β5 (β4-β5) are marked. (b) Contact region 2, showing interactions of MV-H with the CD46 SCR1-SCR2 interdomain region. This surface includes contacts between MV-H and CD46 residues linking Cys60 in SCR1 and Cys65 in SCR2, as well as the DE loop of SCR2. (c) Contact region 3, showing interactions between MV-H and the SCR2 of CD46. The N-acetylglucosamine (NAG) residue attached to Asn80 of CD46 is shown in stick representation with carbons colored green. Additional contacts are listed in Supplementary Table 1.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2010, 17, 124-129) copyright 2010.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23202587 X.Zhang, G.Lu, J.Qi, Y.Li, Y.He, X.Xu, J.Shi, C.W.Zhang, J.Yan, and G.F.Gao (2013).
Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.
  Nat Struct Mol Biol, 20, 67-72.
PDB code: 4gjt
21217701 C.K.Navaratnarajah, N.Oezguen, L.Rupp, L.Kay, V.H.Leonard, W.Braun, and R.Cattaneo (2011).
The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.
  Nat Struct Mol Biol, 18, 128-134.  
21289649 E.O.Saphire, and M.B.Oldstone (2011).
Measles virus fusion shifts into gear.
  Nat Struct Mol Biol, 18, 115-116.  
21217702 T.Hashiguchi, T.Ose, M.Kubota, N.Maita, J.Kamishikiryo, K.Maenaka, and Y.Yanagi (2011).
Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM.
  Nat Struct Mol Biol, 18, 135-141.
PDB codes: 3alw 3alx 3alz
20941397 B.D.Persson, N.B.Schmitz, C.Santiago, G.Zocher, M.Larvie, U.Scheu, J.M.Casasnovas, and T.Stehle (2010).
Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens.
  PLoS Pathog, 6, 0.
PDB code: 3o8e
20736930 C.Frecha, C.Lévy, F.L.Cosset, and E.Verhoeyen (2010).
Advances in the field of lentivector-based transduction of T and B lymphocytes for gene therapy.
  Mol Ther, 18, 1748-1757.  
20375167 T.A.Bowden, M.Crispin, D.J.Harvey, E.Y.Jones, and D.I.Stuart (2010).
Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly.
  J Virol, 84, 6208-6217.
PDB code: 2x9m
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.