1hcn: Difference between revisions
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'''STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN''' | {{Structure | ||
|PDB= 1hcn |SIZE=350|CAPTION= <scene name='initialview01'>1hcn</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HCN is a [ | 1HCN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCN OCA]. | ||
==Reference== | ==Reference== | ||
Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein., Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA, Structure. 1994 Jun 15;2(6):545-58. PMID:[http:// | Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein., Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA, Structure. 1994 Jun 15;2(6):545-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7922031 7922031] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Canfield, R E.]] | [[Category: Canfield, R E.]] | ||
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[[Category: hormone]] | [[Category: hormone]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:19 2008'' | ||
Revision as of 09:35, 20 March 2008
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| 1hcn, resolution 2.6Å | |||||||||||||
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| Ligands: | NAG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
Overview
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.
About this Structure
1HCN is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein., Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA, Structure. 1994 Jun 15;2(6):545-58. PMID:7922031
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