PDBsum entry: 1hcn

Hormone

PDB-id

1hcn


	Asymmetric unit

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Protein chains

Ligands

NAG ×2

Waters ×63

* Residue conservation analysis

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		Biological unit, tetramer (as deduced by PQS)

PDB id:

1hcn

Name:

Hormone

Title:

Structure of human chorionic gonadotropin at 2.6 angstroms resolution 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.

Biological unit:

Tetramer (from PQS)

UniProt:

Chain A: P01215 (GLHA_HUMAN)

Seq:				116 a.a.

Struc:				85 a.a.

Chain B: P01233 (CGHB_HUMAN)

Seq:

165 a.a.

Struc:

110 a.a.

Key:		PfamA domain
		Secondary structure			CATH domain

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

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Key reference

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

18945715 S.F.de Medeiros, and R.J.Norman (2009).
Human choriogonadotrophin protein core and sugar branches heterogeneity: basic and clinical insights.

Hum Reprod Update, 15, 69-95.

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.

J Biol Chem, 284, 10890-10900.

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).
A Necessary and Sufficient Determinant for Protein-selective Glycosylation in Vivo.

J Biol Chem, 283, 1985-1991.

18084009 M.Ghadami, S.A.Salama, N.Khatoon, R.Chilvers, M.Nagamani, P.J.Chedrese, and A.Al-Hendy (2008).
Toward gene therapy of primary ovarian failure: adenovirus expressing human FSH receptor corrects the Finnish C566T mutation.

Mol Hum Reprod, 14, 9.

18274893 V.Blanchard, R.A.Gadkari, A.V.George, S.Roy, G.J.Gerwig, B.R.Leeflang, R.R.Dighe, R.Boelens, and J.P.Kamerling (2008).
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.

Glycoconj J, 25, 245-257.

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.

17287585 K.Miyai (2007).
Congenital thyrotropin deficiency--from discovery to molecular biology, postgenome and preventive medicine.

Endocr J, 54, 191-203.

17158104 P.M.Smallwood, J.Williams, Q.Xu, D.J.Leahy, and J.Nathans (2007).
Mutational analysis of Norrin-Frizzled4 recognition.

J Biol Chem, 282, 4057-4068.

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.

Mol Cell Endocrinol, 260, 83-92.

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.

Thyroid, 14, 991.

15521866 S.D.Keay, M.Vatish, E.Karteris, E.W.Hillhouse, and H.S.Randeva (2004).
The role of hCG in reproductive medicine.

BJOG, 111, 1218-1228.

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.

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.

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.

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.

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.

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.

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.

J Biol Chem, 272, 15532-15540.

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.

J Biol Chem, 272, 21312-21316.

9449027 M.M.Elliott, A.Kardana, J.W.Lustbader, and L.A.Cole (1997).
Carbohydrate and peptide structure of the alpha- and beta-subunits of human chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma.

Endocrine, 7, 15-32.

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.

Biophys J, 73, 1190-1197.

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.

Nat Biotechnol, 15, 439-443.

9081984 R.W.Ruddon, and E.Bedows (1997).
Assisted protein folding.

J Biol Chem, 272, 3125-3128.

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.

Nat Biotechnol, 15, 663-667.

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

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

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.

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

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.

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.

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.

Proteins, 26, 353-357.

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.

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.

Eur J Biochem, 241, 627-632.

9631089 M.W.Szkudlinski, N.G.Teh, M.Grossmann, J.E.Tropea, and B.D.Weintraub (1996).
Engineering human glycoprotein hormone superactive analogues.

Nat Biotechnol, 14, 1257-1263.

8870072 P.Bork, A.K.Downing, B.Kieffer, and I.D.Campbell (1996).
Structure and distribution of modules in extracellular proteins.

Q Rev Biophys, 29, 119-167.

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.

J Biol Chem, 271, 12117-12120.

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.

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.

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.

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.

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.

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).
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7649974 N.Q.McDonald, and M.V.Chao (1995).
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Protein Sci, 3, 1706-1711.

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