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Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein

Authors :
Matthews, David A.
Smith, Ward W.
Ferre, Rose Ann
Condon, Brad
Budahazi, Gregg
Sisson, Wes
Villafranca, J.E.
Janson, Cheryl A.
McElroy, H.E.
Gribskov, C.L.
Worland, Stephen
Source :
Cell. June 3, 1994, Vol. 77 Issue 5, p761, 11 p.
Publication Year :
1994

Abstract

The structure of human rhinovirus-14 3C protease (3Cpro) discloses folds constituting two topologically equivalent six-stranded beta barrels and suggests means for 3CD polyprotein cleavage. Functions of 3Cpro include providing a binding site for RNA binding with catalytic residues. 3Cpro is akin to trypsin-like serine protease in forming folds.

Details

ISSN :
00928674
Volume :
77
Issue :
5
Database :
Gale General OneFile
Journal :
Cell
Publication Type :
Academic Journal
Accession number :
edsgcl.16136132