Structural studies of cysteine proteases and their inhibitors.
Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins.
Grzonka
Z
Z
Department of Organic Chemistry, Faculty of Chemistry, University of Gdańsk, Poland. grzonka@chemik.chem.univ.gda.pl
Jankowska
E
E
Kasprzykowski
F
F
Kasprzykowska
R
R
Lankiewicz
L
L
Wiczk
W
W
Wieczerzak
E
E
Ciarkowski
J
J
Drabik
P
P
Janowski
R
R
Kozak
M
M
Jaskólski
M
M
Grubb
A
A
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D020134:Catalytic Domain; D017124:Conserved Sequence; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases