The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
Article Abstract:
A study examined the crystal structure of the human estrogen receptor alpha (hERalpha) ligand-binding domain (LBD) linked to the agonist diethylstilbestrol and a peptide obtained from the coactivator GRIP1. The study also studied the crystal structure of the hERalpha LBD connected to the selective antagonist 4-hydroxytamoxifen (OHT). The peptide binds as a short alpha helix to a hydrophobic groove on the surface of the LBD in the first complex while helix 12 obstructs the coactivator recognition groove in the second complex. The structures demonstrate two different processes by which structural OHT features promote autoinhibitory helix 12 conformation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Molecular basis for the binding promiscuity of an Anti-p24 (HIV-1) monoclonal antibody
Article Abstract:
A synthetic positional scanning combinatorial library was used to identify five unique peptides that bind the paratope region of the monoclonal antibody CB4-1, an antibody directed against the HIV-1 p24 antigen. Substitution analogs revealed the key residues involved in the interaction. Binding supertopes were derived for each peptide and used to determine possible binding domains in other proteins. The results generated have important implications in the field of autoimmunity and immune escape.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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The biological and chemical basis for tissue-selective amyloid disease
Article Abstract:
A demonstration that mammalian cells secrete numerous transthyretin (TTR) disease-associated variants with wild-type efficiency in spite of compromised folding energetics, is presented. It is proposed that ER-assisted folding (ERAF) in competition with ER-associated degradation (ERAD) defines the unique secretory aptitude of each tissue.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
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- Abstracts: Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
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