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PDBsum entry 1ot5
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Hydrolase/hydrolase inhibitor
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PDB id
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1ot5
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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2.4 a resolution crystal structure of the prototypical hormone-Processing protease kex2 in complex with an ala-Lys-Arg boronic acid inhibitor.
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Authors
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T.Holyoak,
M.A.Wilson,
T.D.Fenn,
C.A.Kettner,
G.A.Petsko,
R.S.Fuller,
D.Ringe.
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Ref.
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Biochemistry, 2003,
42,
6709-6718.
[DOI no: ]
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PubMed id
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Abstract
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This paper reports the first structure of a member of the Kex2/furin family of
eukaryotic pro-protein processing proteases, which cleave sites consisting of
pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal
structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg
inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar
in its global fold to the subtilisin-like superfamily of degradative proteases.
Analysis of the complex provides a structural basis for the extreme selectivity
of this enzyme family that has evolved from a nonspecific subtilisin-like
ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of
nine beta strands and may potentially be involved, along with the buried Ca(2+)
ion, in creating the highly determined binding site for P(1) arginine.
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