Rearranging exosites in noncatalytic domains can redirect the substrate specificity of ADAMTS proteases

Journal of Biological Chemistry

Volumn 287, Issue 32, 2012, Pages 26944-26952

  Gao, Weiqiang ^a   Zhu, Jian ^a   Westfield, Lisa A ^a   Tuley, Elodee A ^a   Anderson, Patricia J ^a   Sadler, J Evan ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL DOMAINS; CLEAVAGE SITES; EXOSITES; FLUID SHEAR STRESS; METALLO-PROTEASE; MULTIMERS; N-TERMINALS; NON-CATALYTIC; PEPTIDE SUBSTRATES; SUBSTRATE RECOGNITION; SUBSTRATE SPECIFICITY; VON WILLEBRAND FACTOR;

AMINO ACIDS; ENZYME ACTIVITY; GLYCOPROTEINS; PHYSIOLOGY;

SUBSTRATES;

AGGRECAN; AGGRECANASE 2; ALANINE; CARBOXY TERMINAL TELOPEPTIDE; CYSTEINE; GLUTAMIC ACID; GLYCINE; ISOLEUCINE; METHIONINE; THROMBOSPONDIN 1; TYROSINE; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

ARTICLE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SPECIFICITY; GENE REARRANGEMENT; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; SHEAR STRESS;

ADAM PROTEINS; AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYTIC DOMAIN; CELL LINE; DNA PRIMERS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEOLYSIS; SUBSTRATE SPECIFICITY; VON WILLEBRAND FACTOR;

BOVINAE;

EID: 84864531097     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.380535     Document Type: Article

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