Stabilized Human Cystatin C Variant L47C/G69C Is a Better Reporter Than the Wild-Type Inhibitor for Characterizing the Thermodynamics of Binding to Cysteine Proteases

2019 ◽  
Vol 38 (5) ◽  
pp. 598-607
Author(s):  
David O. Tovar-Anaya ◽  
L. Irais Vera-Robles ◽  
M. Teresa Vieyra-Eusebio ◽  
Ponciano García-Gutiérrez ◽  
Francisco Reyes-Espinosa ◽  
...  
Keyword(s):  
Cystatin C ◽  
Cysteine Proteases ◽  
Wild Type ◽  
Human Cystatin C ◽  
Human Cystatin

Correction to: Stabilized Human Cystatin C, Variant L47C/G69C, is a Better Reporter than the Wild-type Inhibitor for Characterizing the Thermodynamics of Binding to Cysteine Proteases

2019 ◽  
Vol 38 (5) ◽  
pp. 608-608
Author(s):  
David O. Tovar-Anaya ◽  
L. Irais Vera-Robles ◽  
M. Teresa Vieyra-Eusebio ◽  
Ponciano García-Gutiérrez ◽  
Francisco Reyes-Espinosa ◽  
...  
Keyword(s):  
Cystatin C ◽  
Cysteine Proteases ◽  
Wild Type ◽  
Human Cystatin C ◽  
Human Cystatin

The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants

Biopolymers ◽  
2009 ◽  
Vol 91 (5) ◽  
pp. 373-383 ◽  
Author(s):  
Sylwia Rodziewicz-Motowidło ◽  
Justyna Iwaszkiewicz ◽  
Renata Sosnowska ◽  
Paulina Czaplewska ◽  
Emil Sobolewski ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cystatin C ◽  
Amino Acid Residue ◽  
Wild Type ◽  
Conformational Studies ◽  
Human Cystatin C ◽  
Human Cystatin

Neutrophil chemotactic activity is modulated by human cystatin C, an inhibitor of cysteine proteases

Inflammation ◽  
1990 ◽  
Vol 14 (3) ◽  
pp. 247-258 ◽  
Author(s):  
J. Leung-Tack ◽  
C. Tavera ◽  
J. Martinez ◽  
A. Colle
Keyword(s):  
Cystatin C ◽  
Cysteine Proteases ◽  
Chemotactic Activity ◽  
Human Cystatin C ◽  
Human Cystatin ◽  
Neutrophil Chemotactic Activity

scholarly journals Importance of the evolutionarily conserved glycine residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition

1993 ◽  
Vol 291 (1) ◽  
pp. 123-129 ◽  
Author(s):  
A Hall ◽  
H Dalbøge ◽  
A Grubb ◽  
M Abrahamson
Keyword(s):  
Cystatin C ◽  
Equilibrium Constants ◽  
Terminal Segment ◽  
Site Directed Mutagenesis ◽  
Side Chains ◽  
Wild Type ◽  
Human Cystatin C ◽  
Evolutionarily Conserved ◽  
Cysteine Endopeptidases ◽  
Human Cystatin

Human cystatin C variants in which the evolutionarily conserved Gly-11 residue has been replaced by residues with positively charged (Arg), negatively charged (Glu), bulky hydrophobic (Trp), or small (Ser or Ala) side-chains have been produced by site-directed mutagenesis and expression in Escherichia coli. The five variants were isolated and structurally verified. Their inhibitory properties were compared with those of wild-type recombinant cystatin C by determination of the equilibrium constants for dissociation (Ki) of their complexes with the cysteine endopeptidases papain and human cathepsin B and with the cysteine exopeptidase dipeptidyl peptidase I. The Ser-11 and Ala-11 cystatin C variants displayed Ki values for the two endopeptidases that were approx. 20-fold higher than those of wild-type cystatin C, while the corresponding values for the Trp-11. Arg-11 and Glu-11 variants were increased by a factor of about 2000. In contrast, the Ki values for the interactions of all five variants with the exopeptidase differed from that of wild-type cystatin C by a factor of less than 10. Wild-type cystatin C and the Ser-11, Ala-11 and Glu-11 variants were incubated with neutrophil elastase, which in all cases resulted in the rapid hydrolysis of a single peptide bond, between amino acid residues 10 and 11. The Ki values for the interactions with papain of these three N-terminal-decapeptide-lacking cystatin C variants were 20-50 nM, just one order of magnitude higher than the value for N-terminally truncated wild-type cystatin C, which in turn was similar to the corresponding values for the full-length Glu-11, Arg-11 and Trp-11 variants. These data indicate that the crucial feature of the conserved Gly residue in position 11 of wild-type cystatin C is that this residue, devoid of a side-chain, will allow the N-terminal segment of cystatin C to adopt a conformation suitable for interaction with the substrate-binding pockets of cysteine endopeptidases, resulting in high-affinity binding and efficient inhibition. The functional properties of the remaining part of the proteinase contact area, which is built from more C-terminal inhibitor segments, are not significantly affected even when amino acids with bulky or charged side-chains replace the Gly-11 residue of the N-terminal segment.

scholarly journals Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type

2001 ◽  
Vol 77 (2) ◽  
pp. 628-637 ◽  
Author(s):  
Miguel Calero ◽  
Monika Pawlik ◽  
Claudio Soto ◽  
Eduardo M. Castaño ◽  
Einar M. Sigurdsson ◽  
...  
Keyword(s):  
Cystatin C ◽  
Cerebral Hemorrhage ◽  
Wild Type ◽  
Human Cystatin C ◽  
Human Cystatin

Synthesis and antibacterial properties of peptidyl derivatives and cyclopeptides structurally based upon the inhibitory centre of human cystatin C. Dissociation of antiproteolytic and antibacterial effectsNote

Apmis ◽  
2000 ◽  
Vol 108 (7-8) ◽  
pp. 473-481 ◽  
Author(s):  
FRANCISZEK KASPRZYKOWSKI ◽  
CLAES SCHALEN ◽  
REGINA KASPRZYKOWSKA ◽  
BEATA JASTRZEBSKA ◽  
ANDERS GRUBB
Keyword(s):  
Cystatin C ◽  
Antibacterial Properties ◽  
Human Cystatin C ◽  
Human Cystatin

Affinity Purification and Elimination of Methionine Oxidation in Recombinant Human Cystatin C

1997 ◽  
Vol 11 (1) ◽  
pp. 111-118 ◽  
Author(s):  
Paul J. Berti ◽  
Irena Ekiel ◽  
Peter Lindahl ◽  
Magnus Abrahamson ◽  
Andrew C. Storer
Keyword(s):  
Cystatin C ◽  
Affinity Purification ◽  
Methionine Oxidation ◽  
Human Cystatin C ◽  
Human Cystatin

scholarly journals Application of amide hydrogen/deuterium exchange mass spectrometry for epitope mapping in human cystatin C

Amino Acids ◽  
2016 ◽  
Vol 48 (12) ◽  
pp. 2809-2820 ◽  
Author(s):  
Martyna Prądzińska ◽  
Izabela Behrendt ◽  
Juan Astorga-Wells ◽  
Aleksandr Manoilov ◽  
Roman A. Zubarev ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cystatin C ◽  
Epitope Mapping ◽  
Hydrogen Deuterium Exchange ◽  
Amide Hydrogen ◽  
Exchange Mass Spectrometry ◽  
Human Cystatin C ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Human Cystatin

Towards large scale methods for the selective release of periplasmic human cystatin C from E. coli

1995 ◽  
Vol 9 (3) ◽  
pp. 179-184 ◽  
Author(s):  
F. Chaib ◽  
A. Bernier ◽  
E. Braendli
Keyword(s):  
Cystatin C ◽  
Large Scale ◽  
E Coli ◽  
Human Cystatin C ◽  
Human Cystatin
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