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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Molecular basis of agonism and antagonism in the oestrogen receptor

Article Abstract:

The crystal structures of the ligand-binding domain (LBD) of the oestrogen receptor (ER) in complex with the endogenous oestrogen, 17-beta-oesradiol, and the selective antagonist raloxifene give a molecular basis for the clearly recognizable pharmacophore of the ER and its catholic binding properties. Agonist and antagonist show different binding modes, even though they bind at the same site within the core of the LBD. It appears that the antagonist properties of raloxifene are based on its ability to inhibit the formation of a transcriptionally competent AF-2 conformation.

Author: Hubbard, Roderick E., Gustafsson, Jan-Ake, Greene, Geoffrey L., Dauter, Zbigniew, Brzozowski, Andrzej M., Pike, Ashley C.W., Bonn, Tomas, Engstrom, Owe, Ohman, Lars, Carlquist, Mats
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
Estrogen, Estrogen receptors

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A potent and selective endogenous agonist for the mu-opiate receptor

Article Abstract:

Endogenous agonists have been found in the brain for the enkephalin and dynorphin opiate receptors but none has previously been identified for the mu receptor. Morphine and other analgesic compounds mainly act on the mu opiate receptor. A novel method has isolated two endogenous opoid peptides, termed endomorphin-1 and endomorphin-2, with strong affinities for the mu receptor, which may be natural ligands.

Author: Zadina, James E., Hackler, Laszlo, Ge, Lin-Jun, Kastin, Abba J.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
Physiological aspects, Observations, Brain research, Endorphins

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Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand

Article Abstract:

Research into the crystal structure of the human immunoglobulin-like natural killer cell receptor KIR2DL2 bound to its class I ligand HLA-Cw3 is presented. This work gives a molecular mechanism for the allotypic specificity and peptide recognition by KIR molecules on human natural killer cells.

Author: Boyington, Jeffrey C., Motyka, Shawn A., Schuck, Peter, Brooks, Andrew G., Sun, Peter D.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
Killer cells

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Subjects list: Research, Ligand binding (Biochemistry)
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