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Immune system PDB id
1qfw
Jmol
Contents
Protein chains
87 a.a. *
111 a.a. *
112 a.a. *
112 a.a. *
108 a.a. *
121 a.a. *
Ligands
NAG ×2
* Residue conservation analysis
PDB id:
1qfw
Name: Immune system
Title: Ternary complex of human chorionic gonadotropin with fv anti subunit and fv anti beta subunit
Structure: Gonadotropin alpha subunit. Chain: a. Synonym: hcg. Gonadotrophin beta subunit. Chain: b. Synonym: hcg. Antibody (anti alpha subunit) (light chain). Chain: l. Fragment: fv.
Source: Homo sapiens. Human. Organism_taxid: 9606. Secretion: human pregnancy urine. Other_details: sugar residues linked to asn52 and asn78. Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090
Biol. unit: Hexamer (from PQS)
Resolution:
3.50Å     R-factor:   0.260     R-free:   0.310
Authors: M.Tegoni,S.Spinelli,C.Cambillau
Key ref:
M.Tegoni et al. (1999). Crystal structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits. J Mol Biol, 289, 1375-1385. PubMed id: 10373373 DOI: 10.1006/jmbi.1999.2845
Date:
15-Apr-99     Release date:   26-Apr-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01215  (GLHA_HUMAN) -  Glycoprotein hormones alpha chain
Seq:
Struc: 		116 a.a.
87 a.a.
Protein chain
Pfam   ArchSchema ?
P01233  (CGHB_HUMAN) -  Choriogonadotropin subunit beta
Seq:
Struc: 		165 a.a.
111 a.a.
Protein chain
No UniProt id for this chain
Protein chain
No UniProt id for this chain
Protein chain
No UniProt id for this chain
Protein chain
No UniProt id for this chain
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     developmental growth   15 terms 
  Biochemical function     protein binding     2 terms  

 

 
DOI no: 10.1006/jmbi.1999.2845 J Mol Biol 289:1375-1385 (1999)
PubMed id: 10373373  
 
 
Crystal structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits.
M.Tegoni, S.Spinelli, M.Verhoeyen, P.Davis, C.Cambillau.
 
  ABSTRACT  
 
Human chorionic gonadotropin (hCG), is a placental hormone which exerts its major effect by stimulating progesterone production, crucially sustaining the early weeks of pregnancy. Detection of hCG with specific monoclonal antibodies (mAbs) has become the chosen means for pregnancy diagnosis. We have used antibody Fv fragments derived from two high-affinity mAbs, one against the alpha and the other against the beta-hCG subunit to enable the crystallisation of intact or desialylated hCG. Crystals of a ternary complex composed of Fv anti-alpha/hCG/Fv anti-beta were found to diffract to 3.5 A resolution, and the structure was solved by molecular replacement. In the crystal, the two Fvs keep hCG as in a molecular cage, providing good protein-protein contacts and leaving enough space for the saccharides to be accommodated in the cell solvent. The two Fvs were found not to interact directly through their complementary-determining regions with the hCG saccharides, but only with the protein. The hCG structure in the ternary complex was very close to that of the HF partially deglycosylated hormone, thus indicating that neither the saccharides nor the Fvs had any substantial influence on hormone structure.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Representation of the ternary complex of hCG and the two Fv fragments. The anti-β Fv is at the top, and the anti-α Fv at the bottom. Left, stereo view ribbon representation of the complex; the anti-β Fv VH is pink, and the VL is violet; the anti-α Fv VH is dark blue and the VL is light blue. The hCG α-subunit is red, and β-subunit is orange. GlnNAc-GlcNAc at Asn52 and GlcNAc at Asn78 are represented as CPK spheres. The two main hCG loops interacting with the Fvs (14A-21A and 73A-81A), are labelled. Right, Molecular surface representation of the complex (Fv anti-α, green; Fv anti-β, orange; hCG, purple; sugar, red).
Figure 7.
Figure 7. Stereo view of the F[o] −F[c] sigma electron density map around Asn52. The two first Gluc-NAc moieties attached to this residue are also represented.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1999, 289, 1375-1385) copyright 1999.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20939100 S.Kalkhof, S.Haehn, M.Paulsson, N.Smyth, J.Meiler, and A.Sinz (2010).
Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking.
  Proteins, 78, 3409-3427.  
17059864 D.Puett, Y.Li, G.DeMars, K.Angelova, and F.Fanelli (2007).
A functional transmembrane complex: the luteinizing hormone receptor with bound ligand and G protein.
  Mol Cell Endocrinol, 260, 126-136.  
16603068 J.Huang, and W.Honda (2006).
CED: a conformational epitope database.
  BMC Immunol, 7, 7.  
16467256 D.Puett, Y.Li, K.Angelova, G.Demars, T.P.Meehan, F.Fanelli, and P.Narayan (2005).
Structure-function relationships of the luteinizing hormone receptor.
  Ann N Y Acad Sci, 1061, 41-54.  
15103132 A.McPherson, J.Day, and L.J.Harris (2004).
Crystals of the beta-subunit of bovine luteinizing hormone and indicators for the involvement of proteolysis in protein crystallization.
  Acta Crystallogr D Biol Crystallogr, 60, 872-877.  
15304493 W.R.Moyle, Y.Xing, W.Lin, D.Cao, R.V.Myers, J.E.Kerrigan, and M.P.Bernard (2004).
Model of glycoprotein hormone receptor ligand binding and signaling.
  J Biol Chem, 279, 44442-44459.  
12001233 J.G.Renisio, J.Pérez, M.Czisch, M.Guenneugues, O.Bornet, L.Frenken, C.Cambillau, and H.Darbon (2002).
Solution structure and backbone dynamics of an antigen-free heavy chain variable domain (VHH) from Llama.
  Proteins, 47, 546-555.
PDB code: 1g9e
10913841 R.V.Myers, Y.Wang, and W.R.Moyle (2000).
The surface of alpha-subunit loop 1 distant from the subunit interface is exposed in the hCG lutropin receptor complex.
  Biochim Biophys Acta, 1475, 390-394.  
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.