Cooperativity and Dimerization of Recombinant Human Estrogen Receptor Hormone-binding Domain
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چکیده
منابع مشابه
Cooperativity and dimerization of recombinant human estrogen receptor hormone-binding domain.
The estrogen receptor dimerizes and exhibits cooperative ligand binding as part of its normal functioning. Interaction of the estrogen receptor with its ligands is mediated by a C-terminal hormone-binding domain (HBD), and residues within the HBD are thought to contribute to dimerization. To examine dimer interactions in the isolated HBD, a human estrogen receptor HBD fragment was expressed in ...
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Clostridium Botulinum Type E neurotoxin heavy chain consists of two domains: the translocation domain asthe N-terminal half and the binding domain as the Cterminal half (Hc). One effective way to neutralize botulinum neurotoxin is to inhibit binding of this toxin to neuromuscular synapses with antibodies against binding domain. Two synthetic genes, coding for Hc (the full length binding d...
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It has recently been shown that 20 kDa human growth hormone (hGH) forms the 1:2 hGH:hGH receptor (hGHR) complex and expresses full agonistic activity, although it hardly forms the 1:1 GH:GHR complex as compared with 22 kDa hGH. To clarify this mechanism, we analyzed the mode of receptor dimerization of 20 kDa hGH using the intact form and mutants. Complex formation analysis between hGHR extrace...
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Cooperativity of ligand-receptor binding influences the input-output behavior of a biochemical system and thus is an important determinant of its physiological function. Canonically, such cooperativity is understood in terms of ligand-receptor binding affinity, where an initial binding event changes the affinity for subsequent binding events. Here, we demonstrate that dimerization-a simple yet ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1997
ISSN: 0021-9258
DOI: 10.1074/jbc.272.8.4843