A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation

Biochemical and Biophysical Research Communications

Volumn 366, Issue 3, 2008, Pages 862-867

  Fairhead, Michael ^a   Kelly, Sharon M ^b   van der Walle, Christopher F ^a  

^a UNIVERSITY OF STRATHCLYDE   (United Kingdom)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

Binding motif; Cathepsin L; Circular dichroism; Cysteine protease; Fluorescence; Heparin; Pro domain

Indexed keywords

CATHEPSIN L; ENZYME PRECURSOR; HEPARIN;

ARTICLE; CANCER INVASION; ENZYME ACTIVATION; ENZYME DEGRADATION; ENZYME SUBSTRATE; EXTRACELLULAR MATRIX; MUTATIONAL ANALYSIS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STABILITY; RECEPTOR AFFINITY;

BINDING SITES; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; ENZYME PRECURSORS; HEPARIN; HUMANS; HYDROGEN-ION CONCENTRATION; PICHIA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

EID: 37549071494     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.12.062     Document Type: Article

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