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Anatomy of lipase binding sites: the scissile fatty acid binding site

Chemistry and Physics of Lipids, 1998
Shape and physico-chemical properties of the scissile fatty acid binding sites of six lipases and two serine esterases were analyzed and compared in order to understand the molecular basis of substrate specificity. All eight serine esterases and lipases have similar architecture and catalytic mechanism of ester hydrolysis, but different substrate ...
J, Pleiss, M, Fischer, R D, Schmid
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Melatonin Binding Sites

Journal of Neurochemistry, 1988
Abstract: The distribution and characterization of specific melatonin binding sites were studied using 125I‐melatonin. Autoradiography revealed only three sites of specific melatonin binding in brain: the suprachiasmatic nuclei, the median eminence, and the small part of choroid plexus at the caudal end of the fourth ventricle.
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What makes a binding site a binding site?

Current Opinion in Structural Biology, 1995
Organic probe molecules have recently been used to define hydrophobic binding sites on the surface of proteins. It appears that the presence of water on the surface of a protein plays a crucial role in the interaction between that protein and its binding site.
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Interaction of the dibutylchloromethyltin chloride binding site with the carbodiimide binding site in mitochondria

Biochemical and Biophysical Research Communications, 1980
Abstract An examination of the effect of dibutylchloromethyltin/chloride on the carbodiimide binding proteolipid of mitrochondrial ATPase has revealed that in the presence of the alkyltin, (1) binding of dicyclohexycarbodiimide is decreased (2) the electron spin resonance spectrum of a nitroxide analogue of dicyclohexylcarbodiimide exhibits line ...
M D, Partis   +3 more
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On the receptor binding site of relaxins

International Journal of Peptide and Protein Research, 1988
Relaxin plays a critical role in viviparity and has recently been implicated as a hormone of oviparity as well. In most mammals relaxin causes the widening of the birth canal during parturition and suppresses uterine motility during pregnancy. Relaxins isolated from several species have shown a great deal of sequence variability, and speculations ...
E E, Büllesbach, C, Schwabe
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Mitochondrial Binding Sites for Triiodothyronine

Endocrinology, 1978
Metabolic effects upon rat liver mitochondria have been observed by others within 2 min of injection of massive amounts of L-T4. Reported here is the subcellular distribution of 2--5 ng high specific activity [125I]L-T3 2 min after ip injection with and without a loading dose of 30 micrograms unlabeled T3.
R L, Greif, D, Sloane
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A Binding Site for Chlorambucil on Metallothionein

Biochemistry, 1996
It is of interest to test the hypothesis that induced metallothionein (MT) acts in acquired drug resistance by covalent sequestration. In this study MT was incubated in vitro with chlorambucil (CHB) under conditions where only 1:1 covalent adducts were formed.
J, Zaia   +6 more
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The binding site for C1q on IgG

Nature, 1988
In humoral defence, pathogens are cleared by antibodies acting as adaptor molecules: they bind to antigen and trigger clearance mechanisms such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and complement lysis. The first step in the complement cascade is the binding of C1q to the antibody.
A R, Duncan, G, Winter
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Metal-binding sites in proteins

Current Opinion in Biotechnology, 1991
A dramatic increase in the number of solved metalloprotein structures and recent breakthroughs in structural analysis have provided a sufficiently detailed understanding of the structural chemistry of some metal-binding sites to allow successful design.
J A, Tainer, V A, Roberts, E D, Getzoff
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Protein metal-binding sites

Current Opinion in Biotechnology, 1992
Metal ions have a role in a variety of important functions in proteins including protein folding, assembly, stability, conformational change, and catalysis. The presence or absence of a given metal ion is crucial to the conformation or activity of over one third of all proteins.
J A, Tainer, V A, Roberts, E D, Getzoff
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