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Hormone PDB id
1hcn
Jmol
Contents
Protein chains
85 a.a. *
110 a.a. *
Ligands
NAG ×2
Waters ×63
* Residue conservation analysis
PDB id:
1hcn
Name: Hormone
Title: Structure of human chorionic gonadotropin at 2.6 angstroms r from mad analysis of the selenomethionyl protein
Structure: Human chorionic gonadotropin. Chain: a. Engineered: yes. Human chorionic gonadotropin. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606.
Biol. unit: Tetramer (from PQS)
Resolution:
2.60Å     R-factor:   0.199    
Authors: H.Wu,J.W.Lustbader,Y.Liu,R.E.Canfield,W.A.Hendrickson
Key ref:
H.Wu et al. (1994). Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. Structure, 2, 545-558. PubMed id: 7922031 DOI: 10.1016/S0969-2126(00)00054-X
Date:
01-Jul-94     Release date:   30-Sep-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01215  (GLHA_HUMAN) -  Glycoprotein hormones alpha chain
Seq:
Struc: 		116 a.a.
85 a.a.
Protein chain
Pfam   ArchSchema ?
P01233  (CGHB_HUMAN) -  Choriogonadotropin subunit beta
Seq:
Struc: 		165 a.a.
110 a.a.
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     hormone activity     1 term  

 

 
DOI no: 10.1016/S0969-2126(00)00054-X Structure 2:545-558 (1994)
PubMed id: 7922031  
 
 
Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein.
H.Wu, J.W.Lustbader, Y.Liu, R.E.Canfield, W.A.Hendrickson.
 
  ABSTRACT  
 
BACKGROUND: Human chorionic gonadotropin (hCG) is a placental hormone that stimulates secretion of the pregnancy-sustaining steroid progesterone. It is a member of a family of glycoprotein hormones that are disulfide-rich heterodimers, with a common alpha-chain and distinctive beta-chains specific to their particular G-protein linked receptors. RESULTS: We have produced recombinant hCG in mammalian cells as the selenomethionyl protein, and have determined its structure (after partial deglycosylation) at 2.6 A resolution from multiwavelength anomalous diffraction (MAD) measurements. Despite only limited sequence similarity (10% identity), the alpha- and beta-subunits of hCG have similar tertiary folds. Each subunit has a cystine-knot motif at its core of extended hairpin loops. There is a very extensive subunit interface featuring two inter-chain beta-sheets and a unique, disulfide-tethered 'arm' from the beta-subunit which 'embraces' the alpha-subunit. The carboxy-terminal peptide of the beta-subunit, which is rich in O-linked sugars, is disordered. CONCLUSIONS: Structural and sequence comparisons indicate an evolutionary homology, albeit remote, between the glycoprotein hormone chains and other cystine-knot proteins, notably platelet-derived growth factor. Segments of the alpha- and beta-chains that have been convincingly implicated in receptor binding by hCG are juxtaposed on one side of the molecule. A glycosylation site implicated in signal transduction but not in binding is also close to the presumed binding site suggesting a possible coupling between ligand binding and signaling. This study with selenomethionyl protein produced in mammalian cells extends the realm of MAD phasing.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. A portion of the MAD-phased map and (b) the current 2 F[o] – F[c] map superimposed with the model refined at 2.6 å resolution. Electron density is contoured at 1.0σ (blue) and 5.5σ (red). Two prominent features are the N-acetylglucosamine residue attached to Asn52, and Met47 in the hCG α-subunit. Figure 1. A portion of the MAD-phased map and (b) the current 2 [3]mid F[o] [4]mid – [5]mid F[c] [6]mid map superimposed with the model refined at 2.6 å resolution. Electron density is contoured at 1.0σ (blue) and 5.5σ (red). Two prominent features are the N-acetylglucosamine residue attached to Asn52, and Met47 in the hCG α-subunit.
Figure 3.
Figure 3. A schematic drawing of the hCG dimer topology. Figure 3. A schematic drawing of the hCG dimer topology.
 
  The above figures are reprinted by permission from Cell Press: Structure (1994, 2, 545-558) copyright 1994.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20735820 L.A.Cole (2010).
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Selenomethionine incorporation in proteins expressed in Lactococcus lactis.
  Protein Sci, 18, 1121-1127.
PDB code: 3fto
18945715 S.F.de Medeiros, and R.J.Norman (2009).
Human choriogonadotrophin protein core and sugar branches heterogeneity: basic and clinical insights.
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19208630 V.Veverka, A.J.Henry, P.M.Slocombe, A.Ventom, B.Mulloy, F.W.Muskett, M.Muzylak, K.Greenslade, A.Moore, L.Zhang, J.Gong, X.Qian, C.Paszty, R.J.Taylor, M.K.Robinson, and M.D.Carr (2009).
Characterization of the Structural Features and Interactions of Sclerostin: MOLECULAR INSIGHT INTO A KEY REGULATOR OF Wnt-MEDIATED BONE FORMATION.
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PDB code: 2k8p
18048353 E.Miller, D.Fiete, N.M.Blake, M.Beranek, E.L.Oates, Y.Mi, D.S.Roseman, and J.U.Baenziger (2008).
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High-level expression of biologically active glycoprotein hormones in Pichia pastoris strains--selection of strain GS115, and not X-33, for the production of biologically active N-glycosylated 15N-labeled phCG.
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17059864 D.Puett, Y.Li, G.DeMars, K.Angelova, and F.Fanelli (2007).
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17358049 J.A.Wilken, and E.Bedows (2007).
A novel four-amino acid determinant defines conformational freedom within chorionic gonadotropin beta-subunits.
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17287585 K.Miyai (2007).
Congenital thyrotropin deficiency--from discovery to molecular biology, postgenome and preventive medicine.
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17158104 P.M.Smallwood, J.Williams, Q.Xu, D.J.Leahy, and J.Nathans (2007).
Mutational analysis of Norrin-Frizzled4 recognition.
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17045735 Q.R.Fan, and W.A.Hendrickson (2007).
Assembly and structural characterization of an authentic complex between human follicle stimulating hormone and a hormone-binding ectodomain of its receptor.
  Mol Cell Endocrinol, 260, 73-82.  
17143726 S.R.Setlur, and R.R.Dighe (2007).
Single chain human chorionic gonadotropin, hCGalphabeta: effects of mutations in the alpha subunit on structure and bioactivity.
  Glycoconj J, 24, 97.  
17059863 W.Lin, M.P.Bernard, D.Cao, R.V.Myers, J.E.Kerrigan, and W.R.Moyle (2007).
Follitropin receptors contain cryptic ligand binding sites.
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16880207 J.Sun, F.F.Zhuang, J.E.Mullersman, H.Chen, E.J.Robertson, D.Warburton, Y.H.Liu, and W.Shi (2006).
BMP4 activation and secretion are negatively regulated by an intracellular gremlin-BMP4 interaction.
  J Biol Chem, 281, 29349-29356.  
16823037 W.A.Barton, D.Tzvetkova-Robev, H.Erdjument-Bromage, P.Tempst, and D.B.Nikolov (2006).
Highly efficient selenomethionine labeling of recombinant proteins produced in mammalian cells.
  Protein Sci, 15, 2008-2013.  
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.  
15662415 Q.R.Fan, and W.A.Hendrickson (2005).
Structure of human follicle-stimulating hormone in complex with its receptor.
  Nature, 433, 269-277.
PDB code: 1xwd
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.  
15304512 M.P.Bernard, W.Lin, D.Cao, R.V.Myers, Y.Xing, and W.R.Moyle (2004).
Only a portion of the small seatbelt loop in human choriogonadotropin appears capable of contacting the lutropin receptor.
  J Biol Chem, 279, 44438-44441.  
15650352 R.Núñez Miguel, J.Sanders, J.Jeffreys, H.Depraetere, M.Evans, T.Richards, T.L.Blundell, B.Rees Smith, and J.Furmaniak (2004).
Analysis of the thyrotropin receptor-thyrotropin interaction by comparative modeling.
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15521866 S.D.Keay, M.Vatish, E.Karteris, E.W.Hillhouse, and H.S.Randeva (2004).
The role of hCG in reproductive medicine.
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15161903 Y.Xing, R.V.Myers, D.Cao, W.Lin, M.Jiang, M.P.Bernard, and W.R.Moyle (2004).
Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive beta-subunit disulfide switch.
  J Biol Chem, 279, 35437-35448.  
15161904 Y.Xing, R.V.Myers, D.Cao, W.Lin, M.Jiang, M.P.Bernard, and W.R.Moyle (2004).
Glycoprotein hormone assembly in the endoplasmic reticulum: III. The seatbelt and its latch site determine the assembly pathway.
  J Biol Chem, 279, 35449-35457.  
15161918 Y.Xing, R.V.Myers, D.Cao, W.Lin, M.Jiang, M.P.Bernard, and W.R.Moyle (2004).
Glycoprotein hormone assembly in the endoplasmic reticulum: I. The glycosylated end of human alpha-subunit loop 2 is threaded through a beta-subunit hole.
  J Biol Chem, 279, 35426-35436.  
15166248 Y.Xing, R.V.Myers, D.Cao, W.Lin, M.Jiang, M.P.Bernard, and W.R.Moyle (2004).
Glycoprotein hormone assembly in the endoplasmic reticulum: IV. Probable mechanism of subunit docking and completion of assembly.
  J Biol Chem, 279, 35458-35468.  
15304492 Y.Xing, W.Lin, M.Jiang, D.Cao, R.V.Myers, M.P.Bernard, and W.R.Moyle (2004).
Use of protein knobs to characterize the position of conserved alpha-subunit regions in lutropin receptor complexes.
  J Biol Chem, 279, 44427-44437.  
12773385 G.Smits, M.Campillo, C.Govaerts, V.Janssens, C.Richter, G.Vassart, L.Pardo, and S.Costagliola (2003).
Glycoprotein hormone receptors: determinants in leucine-rich repeats responsible for ligand specificity.
  EMBO J, 22, 2692-2703.  
12963710 J.Sohn, H.Youn, M.Jeoung, Y.Koo, C.Yi, I.Ji, and T.H.Ji (2003).
Orientation of follicle-stimulating hormone (FSH) subunits complexed with the FSH receptor. Beta subunit toward the N terminus of exodomain and alpha subunit to exoloop 3.
  J Biol Chem, 278, 47868-47876.  
11501762 A.Amoresano, S.Orrù, R.A.Siciliano, E.De Luca, R.Napoleoni, A.Sirna, and P.Pucci (2001).
Assignment of the complete disulphide bridge pattern in the human recombinant follitropin beta-chain.
  Biol Chem, 382, 961-968.  
11412304 M.D.Chiesa, P.M.Martensen, C.Simmons, N.Porakishvili, J.Justesen, G.Dougan, I.M.Roitt, P.J.Delves, and T.Lund (2001).
Refocusing of B-cell responses following a single amino acid substitution in an antigen.
  Immunology, 103, 172-178.  
11148053 R.J.Darling, J.A.Wilken, R.W.Ruddon, and E.Bedows (2001).
Intracellular folding pathway of the cystine knot-containing glycoprotein hormone alpha-subunit.
  Biochemistry, 40, 577-585.  
  11167125 V.Garcia-Campayo, and I.Boime (2001).
Novel recombinant gonadotropins.
  Trends Endocrinol Metab, 12, 72-77.  
11526210 Y.Liu, C.M.Ogata, and W.A.Hendrickson (2001).
Multiwavelength anomalous diffraction analysis at the M absorption edges of uranium.
  Proc Natl Acad Sci U S A, 98, 10648-10653.  
11266609 Y.Xing, C.Williams, R.K.Campbell, S.Cook, M.Knoppers, T.Addona, V.Altarocca, and W.R.Moyle (2001).
Threading of a glycosylated protein loop through a protein hole: implications for combination of human chorionic gonadotropin subunits.
  Protein Sci, 10, 226-235.  
11591722 Y.Xing, W.Lin, M.Jiang, R.V.Myers, D.Cao, M.P.Bernard, and W.R.Moyle (2001).
Alternatively folded choriogonadotropin analogs. Implications for hormone folding and biological activity.
  J Biol Chem, 276, 46953-46960.  
10992290 M.T.Hearn, and P.T.Gomme (2000).
Molecular architecture and biorecognition processes of the cystine knot protein superfamily: part I. The glycoprotein hormones.
  J Mol Recognit, 13, 223-278.  
10821673 P.J.Erbel, Y.Karimi-Nejad, J.A.van Kuik, R.Boelens, J.P.Kamerling, and J.F.Vliegenthart (2000).
Effects of the N-linked glycans on the 3D structure of the free alpha-subunit of human chorionic gonadotropin.
  Biochemistry, 39, 6012-6021.
PDB codes: 1e9j 1hd4
10809777 R.J.Darling, R.W.Ruddon, F.Perini, and E.Bedows (2000).
Cystine knot mutations affect the folding of the glycoprotein hormone alpha-subunit. Differential secretion and assembly of partially folded intermediates.
  J Biol Chem, 275, 15413-15421.  
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.  
10766799 V.Singh, and W.E.Merz (2000).
Disulfide bond formation is not required for human chorionic gonadotropin subunit association. Studies with dithiothreitol in JEG-3 cells.
  J Biol Chem, 275, 11765-11770.  
10103036 J.C.Heikoop, B.Huisman-de Winkel, and P.D.Grootenhuis (1999).
Towards minimized gonadotropins with full bioactivity.
  Eur J Biochem, 261, 81-84.  
  10574801 J.J.Bellizzi, J.Widom, C.W.Kemp, and J.Clardy (1999).
Producing selenomethionine-labeled proteins with a baculovirus expression vector system.
  Structure, 7, R263-R267.  
  10484290 L.Lobel, S.Pollak, S.Wang, M.Chaney, and J.W.Lustbader (1999).
Expression and characterization of recombinant beta-subunit hCG homodimer.
  Endocrine, 10, 261-270.  
10651281 M.L.Kouwijzer, H.J.Berendsen, and P.D.Grootenhuis (1999).
Computer simulations of the dynamics of human choriogonadotropin and its alpha subunit.
  Proteins, 37, 668-682.  
10095786 P.J.Erbel, Y.Karimi-Nejad, T.De Beer, R.Boelens, J.P.Kamerling, and J.F.Vliegenthart (1999).
Solution structure of the alpha-subunit of human chorionic gonadotropin.
  Eur J Biochem, 260, 490-498.
PDB code: 1dz7
10517159 P.T.Gomme, P.E.Thompson, J.Whisstock, P.G.Stanton, and M.T.Hearn (1999).
Characterization of epitope regions of thyrotropin beta-subunit recognized by the monoclonal antibodies mAb279 and mAb299: a chimeric peptide approach.
  J Pept Res, 54, 218-229.  
10423550 R.A.Silva, S.A.Sherman, and T.A.Keiderling (1999).
Beta-hairpin stabilization in a 28-residue peptide derived from the beta-subunit sequence of human chorionic gonadotropin hormone.
  Biopolymers, 50, 413-423.  
9712877 C.Fotinou, J.Beauchamp, P.Emsley, A.deHaan, W.J.Schielen, E.Bos, and N.W.Isaacs (1998).
Structure of an Fab fragment against a C-terminal peptide of hCG at 2.0 A resolution.
  J Biol Chem, 273, 22515-22518.
PDB code: 1sbs
9761910 C.Fotinou, J.Beauchamp, P.Emsley, I.Black, A.DeHaan, E.Bos, and N.W.Isaacs (1998).
Crystallization of two hCG-specific monoclonal antibody fragments.
  Acta Crystallogr D Biol Crystallogr, 54, 405-406.  
9699612 C.M.Ogata (1998).
MAD phasing grows up.
  Nat Struct Biol, 5, 638-640.  
  9687376 J.L.Smith, and A.Thompson (1998).
Reactivity of selenomethionine--dents in the magic bullet?
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10022761 K.Shao, S.V.Balasubramanian, C.M.Pope, and O.P.Bahl (1998).
Effect of individual N-glycosyl chains in the beta-subunit on the conformation of human choriogonadotropin.
  Mol Cell Endocrinol, 146, 39-48.  
9743123 M.Grossmann, H.Leitolf, B.D.Weintraub, and M.W.Szkudlinski (1998).
A rational design strategy for protein hormone superagonists.
  Nat Biotechnol, 16, 871-875.  
9558473 M.L.Dufau (1998).
The luteinizing hormone receptor.
  Annu Rev Physiol, 60, 461-496.  
9665835 N.Chabbert Buffet, C.Djakoure, S.C.Maitre, and P.Bouchard (1998).
Regulation of the human menstrual cycle.
  Front Neuroendocrinol, 19, 151-186.  
9593729 T.Phang, G.Kundu, S.Hong, I.Ji, and T.H.Ji (1998).
The amino-terminal region of the luteinizing hormone/choriogonadotropin receptor contacts both subunits of human choriogonadotropin. II. Photoaffinity labeling.
  J Biol Chem, 273, 13841-13847.  
  9165082 A.Bergner, T.Muta, S.Iwanaga, H.G.Beisel, R.Delotto, and W.Bode (1997).
Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain.
  Biol Chem, 378, 283-287.  
9218442 A.Sato, E.Perlas, D.Ben-Menahem, M.Kudo, M.R.Pixley, M.Furuhashi, A.J.Hsueh, and I.Boime (1997).
Cystine knot of the gonadotropin alpha subunit is critical for intracellular behavior but not for in vitro biological activity.
  J Biol Chem, 272, 18098-18103.  
9183002 J.C.Heikoop, M.M.van Beuningen-de Vaan, P.van den Boogaart, and P.D.Grootenhuis (1997).
Evaluation of subunit truncation and the nature of the spacer for single chain human gonadotropins.
  Eur J Biochem, 245, 656-662.  
9219269 J.C.Heikoop, P.van den Boogaart, J.W.Mulders, and P.D.Grootenhuis (1997).
Structure-based design and protein engineering of intersubunit disulfide bonds in gonadotropins.
  Nat Biotechnol, 15, 658-662.  
9467819 L.A.Cole, D.Cermik, and R.Bahado-Singh (1997).
Oligosaccharide variants of hCG-related molecules: potential screening markers for Down syndrome.
  Prenat Diagn, 17, 1188-1190.  
9249860 L.A.Cole, L.H.Kellner, T.Isozaki, G.E.Palomaki, R.K.Iles, R.P.Walker, M.Ozaki, and J.A.Canick (1997).
Comparison of 12 assays for detecting hCG and related molecules in urine samples from Down syndrome pregnancies.
  Prenat Diagn, 17, 607-614.  
9013570 L.Cosowsky, W.Lin, Y.Han, M.P.Bernard, R.K.Campbell, and W.R.Moyle (1997).
Influence of subunit interactions on lutropin specificity. Implications for studies of glycoprotein hormone function.
  J Biol Chem, 272, 3309-3314.  
9182589 M.Grossmann, M.W.Szkudlinski, R.Wong, J.A.Dias, T.H.Ji, and B.D.Weintraub (1997).
Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) beta-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH.
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9261143 M.Grossmann, R.Wong, M.W.Szkudlinski, and B.D.Weintraub (1997).
Human thyroid-stimulating hormone (hTSH) subunit gene fusion produces hTSH with increased stability and serum half-life and compensates for mutagenesis-induced defects in subunit association.
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Carbohydrate and peptide structure of the alpha- and beta-subunits of human chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma.
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9284286 N.Grewal, S.Nagpal, G.B.Chavali, S.S.Majumdar, R.Pal, and D.M.Salunke (1997).
Ligand-induced receptor dimerization may be critical for signal transduction by choriogonadotropin.
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9131622 R.K.Campbell, E.R.Bergert, Y.Wang, J.C.Morris, and W.R.Moyle (1997).
Chimeric proteins can exceed the sum of their parts: implications for evolution and protein design.
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9081984 R.W.Ruddon, and E.Bedows (1997).
Assisted protein folding.
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9219270 V.Garcia-Campayo, A.Sato, B.Hirsch, T.Sugahara, M.Muyan, A.J.Hsueh, and I.Boime (1997).
Design of stable biologically active recombinant lutropin analogs.
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9207067 Y.A.Muller, B.Li, H.W.Christinger, J.A.Wells, B.C.Cunningham, and A.M.de Vos (1997).
Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site.
  Proc Natl Acad Sci U S A, 94, 7192-7197.
PDB code: 1vpf
  9351807 Y.A.Muller, H.W.Christinger, B.A.Keyt, and A.M.de Vos (1997).
The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding.
  Structure, 5, 1325-1338.
PDB code: 2vpf
  9003754 A.Bergner, V.Oganessyan, T.Muta, S.Iwanaga, D.Typke, R.Huber, and W.Bode (1996).
Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor.
  EMBO J, 15, 6789-6797.
PDB code: 1aoc
8887120 A.M.Jackson, T.Klonisch, A.J.Lapthorn, P.Berger, N.W.Isaacs, P.J.Delves, T.Lund, and I.M.Roitt (1996).
Identification and selective destruction of shared epitopes in human chorionic gonadotropin beta subunit.
  J Reprod Immunol, 31, 21-36.  
8940183 C.Wu, P.Narayan, and D.Puett (1996).
Protein engineering of a novel constitutively active hormone-receptor complex.
  J Biol Chem, 271, 31638-31642.  
8548820 D.J.Leahy, I.Aukhil, and H.P.Erickson (1996).
2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.
  Cell, 84, 155-164.
PDB code: 1fnf
8570652 D.L.Griffith, P.C.Keck, T.K.Sampath, D.C.Rueger, and W.D.Carlson (1996).
Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily.
  Proc Natl Acad Sci U S A, 93, 878-883.
PDB code: 1bmp
9027343 D.Puett, N.Bhowmick, L.M.Fernandez, J.Huang, C.Wu, and P.Narayan (1996).
hCG-receptor binding and transmembrane signaling.
  Mol Cell Endocrinol, 125, 55-64.  
8626648 G.C.Kundu, I.Ji, D.J.McCormick, and T.H.Ji (1996).
Photoaffinity labeling of the lutropin receptor with synthetic peptide for carboxyl terminus of the human choriogonadotropin alpha subunit.
  J Biol Chem, 271, 11063-11066.  
9027339 G.R.Bousfield, V.Y.Butnev, R.R.Gotschall, V.L.Baker, and W.T.Moore (1996).
Structural features of mammalian gonadotropins.
  Mol Cell Endocrinol, 125, 3.  
8941011 H.F.Acevedo, and R.J.Hartsock (1996).
Metastatic phenotype correlates with high expression of membrane-associated complete beta-human chorionic gonadotropin in vivo.
  Cancer, 78, 2388-2399.  
8913682 H.S.Pappa, A.E.Stewart, and N.Q.McDonald (1996).
Incorporating anomalous scattering centres into macromolecules.
  Curr Opin Struct Biol, 6, 611-616.  
8953654 H.W.Christinger, Y.A.Muller, L.T.Berleau, B.A.Keyt, B.C.Cunningham, N.Ferrara, and A.M.de Vos (1996).
Crystallization of the receptor binding domain of vascular endothelial growth factor.
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9027342 J.A.Dias (1996).
Human follitropin heterodimerization and receptor binding structural motifs: identification and analysis by a combination of synthetic peptide and mutagenesis approaches.
  Mol Cell Endocrinol, 125, 45-54.  
9027346 J.J.Remy, L.Couture, J.Pantel, T.Haertlé, H.Rabesona, V.Bozon, E.Pajot-Augy, P.Robert, F.Troalen, R.Salesse, and J.M.Bidart (1996).
Mapping of HCG-receptor complexes.
  Mol Cell Endocrinol, 125, 79-91.  
9027340 J.W.Lustbader, S.Pollak, L.Lobel, I.Trakht, S.Homans, J.M.Brown, and R.E.Canfield (1996).
Three-dimensional structures of gonadotropins.
  Mol Cell Endocrinol, 125, 21-31.  
8895101 K.C.Peng, G.R.Bousfield, D.Puett, and D.N.Ward (1996).
Circular dichroic spectroscopy of Arg46-nicked ovine lutropin alpha and derived fragments.
  J Protein Chem, 15, 547-552.  
9027347 K.S.Ryu, I.Ji, L.Chang, and T.H.Ji (1996).
Molecular mechanism of LH/CG receptor activation.
  Mol Cell Endocrinol, 125, 93.  
8902847 K.Shao, S.Purohit, and O.P.Bahl (1996).
Effect of modification of all loop regions in the alpha- and beta-subunits of human choriogonadotropin on its signal transduction activity.
  Mol Cell Endocrinol, 122, 173-182.  
8917465 L.Couture, J.J.Remy, H.Rabesona, F.Troalen, E.Pajot-Augy, V.Bozon, T.Haertle, J.M.Bidart, and R.Salesse (1996).
A defined epitope on the human choriogonadotropin alpha-subunit interacts with the second extracellular loop of the transmembrane domain of the lutropin/choriogonadotropin receptor.
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9631089 M.W.Szkudlinski, N.G.Teh, M.Grossmann, J.E.Tropea, and B.D.Weintraub (1996).
Engineering human glycoprotein hormone superactive analogues.
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9027344 N.el Tayar (1996).
Advances in the molecular understanding of gonadotropins-receptors interactions.
  Mol Cell Endocrinol, 125, 65-70.  
9027341 P.Berger, J.M.Bidart, P.S.Delves, S.Dirnhofer, R.Hoermann, N.Isaacs, A.Jackson, T.Klonisch, A.Lapthorn, T.Lund, K.Mann, I.Roitt, S.Schwarz, and G.Wick (1996).
Immunochemical mapping of gonadotropins.
  Mol Cell Endocrinol, 125, 33-43.  
8870072 P.Bork, A.K.Downing, B.Kieffer, and I.D.Campbell (1996).
Structure and distribution of modules in extracellular proteins.
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9631081 R.W.Ruddon (1996).
Super hormones.
  Nat Biotechnol, 14, 1224.  
  8844836 R.W.Ruddon, S.A.Sherman, and E.Bedows (1996).
Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit.
  Protein Sci, 5, 1443-1452.  
8647799 S.M.Manzella, L.V.Hooper, and J.U.Baenziger (1996).
Oligosaccharides containing beta 1,4-linked N-acetylgalactosamine, a paradigm for protein-specific glycosylation.
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8784347 S.Spinelli, L.Frenken, D.Bourgeois, L.de Ron, W.Bos, T.Verrips, C.Anguille, C.Cambillau, and M.Tegoni (1996).
The crystal structure of a llama heavy chain variable domain.
  Nat Struct Biol, 3, 752-757.
PDB code: 1hcv
8898911 T.De Beer, C.W.Van Zuylen, B.R.Leeflang, K.Hård, R.Boelens, R.Kaptein, J.P.Kamerling, and J.F.Vliegenthart (1996).
NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit.
  Eur J Biochem, 241, 229-242.  
9027345 T.Sugahara, P.D.Grootenhuis, A.Sato, M.Kudo, D.Ben-Menahem, M.R.Pixley, A.J.Hsueh, and I.Boime (1996).
Expression of biologically active fusion genes encoding the common alpha subunit and either the CG beta or FSH beta subunits: role of a linker sequence.
  Mol Cell Endocrinol, 125, 71-77.  
8856063 W.D.Fairlie, P.G.Stanton, and M.T.Hearn (1996).
Contribution of specific disulphide bonds to two epitopes of thyrotropin beta-subunit associated with receptor recognition.
  Eur J Biochem, 240, 622-627.  
  8925835 Y.Koide, H.Papkoff, and H.Kawauchi (1996).
Complete amino acid sequences of follitropin and lutropin in the ostrich, Struthio camelus.
  Eur J Biochem, 240, 262-267.  
7601089 A.R.Bernard, T.N.Wells, A.Cleasby, F.Borlat, M.A.Payton, and A.E.Proudfoot (1995).
Selenomethionine labelling of phosphomannose isomerase changes its kinetic properties.
  Eur J Biochem, 230, 111-118.  
  8535781 A.V.Kajava, G.Vassart, and S.J.Wodak (1995).
Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats.
  Structure, 3, 867-877.  
7831319 B.J.Mengeling, S.M.Manzella, and J.U.Baenziger (1995).
A cluster of basic amino acids within an alpha-helix is essential for alpha-subunit recognition by the glycoprotein hormone N-acetylgalactosaminyltransferase.
  Proc Natl Acad Sci U S A, 92, 502-506.  
7583641 B.Kobe, and J.Deisenhofer (1995).
Proteins with leucine-rich repeats.
  Curr Opin Struct Biol, 5, 409-416.  
7544284 C.W.Van Zuylen, T.De Beer, G.J.Rademaker, J.Haverkamp, J.E.Thomas-Oates, K.Hård, J.P.Kamerling, and J.F.Vliegenthart (1995).
Site-specific and complete enzymic deglycosylation of the native human chorionic gonadotropin alpha-subunit.
  Eur J Biochem, 231, 754-760.  
  8747466 F.K.Athappilly, and W.A.Hendrickson (1995).
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.
  Structure, 3, 1407-1419.
PDB code: 1bdo
8530405 J.Huang, and D.Puett (1995).
Identification of two amino acid residues on the extracellular domain of the lutropin/choriogonadotropin receptor important in signaling.
  J Biol Chem, 270, 30023-30028.  
7493973 M.Grossmann, M.W.Szkudlinski, J.E.Tropea, L.A.Bishop, N.R.Thotakura, P.R.Schofield, and B.D.Weintraub (1995).
Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites. Characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity.
  J Biol Chem, 270, 29378-29385.  
7568073 M.W.Szkudlinski, N.R.Thotakura, and B.D.Weintraub (1995).
Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: role of terminal residues of alpha- and beta-subunit oligosaccharides in metabolic clearance and bioactivity.
  Proc Natl Acad Sci U S A, 92, 9062-9066.  
7649974 N.Q.McDonald, and M.V.Chao (1995).
Structural determinants of neurotrophin action.
  J Biol Chem, 270, 19669-19672.  
7583638 N.W.Isaacs (1995).
Cystine knots.
  Curr Opin Struct Biol, 5, 391-395.  
7548959 P.Laidler, D.A.Cowan, R.C.Hider, A.Keane, and A.T.Kicman (1995).
Tryptic mapping of human chorionic gonadotropin by matrix-assisted laser desorption/ionization mass spectrometry.
  Rapid Commun Mass Spectrom, 9, 1021-1026.  
8674812 P.Ren, M.R.Sairam, and T.A.Yarney (1995).
Bacterial expression of human chorionic gonadotropin alpha subunit: studies on refolding, dimer assembly and interaction with two different beta subunits.
  Mol Cell Endocrinol, 113, 39-51.  
7545167 S.M.Manzella, S.M.Dharmesh, M.C.Beranek, P.Swanson, and J.U.Baenziger (1995).
Evolutionary conservation of the sulfated oligosaccharides on vertebrate glycoprotein hormones that control circulatory half-life.
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7589781 S.Slaughter, Y.Wang, R.V.Myers, and W.R.Moyle (1995).
The lutropin beta-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity.
  Mol Cell Endocrinol, 112, 21-25.  
7705351 W.D.Fairlie, P.G.Stanton, and M.T.Hearn (1995).
Delineation of tyrosine-containing epitopes within the beta subunit of bovine thyrotropin.
  Eur J Biochem, 228, 373-380.  
  8747461 X.Jiang, M.Dreano, D.R.Buckler, S.Cheng, A.Ythier, H.Wu, W.A.Hendrickson, and N.el Tayar (1995).
Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions.
  Structure, 3, 1341-1353.
PDB codes: 1lut 1xul 1xum 1xun
  7704524 D.W.Rodgers (1994).
Cryocrystallography.
  Structure, 2, 1135-1140.  
  7849587 H.E.Aronson, W.E.Royer, and W.A.Hendrickson (1994).
Quantification of tertiary structural conservation despite primary sequence drift in the globin fold.
  Protein Sci, 3, 1706-1711.  
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