1hcn: Difference between revisions
New page: left|200px<br /> <applet load="1hcn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hcn, resolution 2.6Å" /> '''STRUCTURE OF HUMAN C... |
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'''STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br /> | '''STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HCN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1HCN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hormone]] | [[Category: hormone]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:51 2008'' | ||
Revision as of 16:55, 15 February 2008
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STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 ANGSTROMS RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
OverviewOverview
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 StructureAbout this Structure
1HCN is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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