Electrostatic recognition in substrate binding to serine proteases
نویسندگان
چکیده
منابع مشابه
Substrate recognition drives the evolution of serine proteases.
A method is introduced to identify amino acid residues that dictate the functional diversity acquired during evolution in a protein family. Using over 80 enzymes of the chymotrypsin family, we demonstrate that the general organization of the phylogenetic tree and its functional branch points are fully accounted for by a limited number of residues that cluster around the active site of the prote...
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Members of the same protease family show different substrate specificity, even if they share identical folds, depending on the physiological processes they are part of. Here, we investigate the key factors for subpocket and global specificity of factor Xa, elastase, and granzyme B which despite all being serine proteases and sharing the chymotrypsin-fold show distinct substrate specificity prof...
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It is generally accepted that the major autoantigen for antiphospholipid antibodies (aPL) in the antiphospholipid syndrome (APS) is beta(2)-glycoprotein I (beta(2)GPI). However, a recent study has revealed that some aPL bind to certain conformational epitope(s) on beta(2)GPI shared by the homologous enzymatic domains of several serine proteases involved in hemostasis and fibrinolysis. Important...
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Proteases regulate numerous biological processes with a degree of specificity often dictated by the amino acid sequence of the substrate cleavage site. To map protease/substrate interactions, a 722-member library of fluorogenic protease substrates of the general format Ac-Ala-X-X-(Arg/Lys)-coumarin was synthesized (X=all natural amino acids except cysteine) and microarrayed with fluorescent cal...
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ژورنال
عنوان ژورنال: Journal of Molecular Recognition
سال: 2018
ISSN: 0952-3499
DOI: 10.1002/jmr.2727