Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations.

Protein science : a publication of the Protein Society

Volumn 18, Issue 5, 2009, Pages 1081-1094

  Spraggon, Glen ^a   Hornsby, Michael ^a   Shipway, Aaron ^a   Tully, David C ^a   Bursulaya, Badry ^a   Danahay, Henry ^a   Harris, Jennifer L ^a   Lesley, Scott A ^a  

^a GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA-CHYMOTRYPSIN; APROTININ; CALCIUM; CAMOSTAT MESILATE; CHYMOTRYPSIN; CHYMOTRYPSIN A; DIVALENT CATION; DRUG DERIVATIVE; GABEXATE; PROSTASIN; PROTEINASE INHIBITOR; SERINE PROTEINASE;

ARTICLE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

APROTININ; CALCIUM; CATALYTIC DOMAIN; CATIONS, DIVALENT; CHYMOTRYPSIN; CRYSTALLOGRAPHY, X-RAY; GABEXATE; HUMANS; PROTEASE INHIBITORS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 68849090838     PISSN: None     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.118     Document Type: Article

References (0)