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PDBsum entry 2er0
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Hydrolase/hydrolase inhibitor
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PDB id
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2er0
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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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X-Ray studies of aspartic proteinase-Statine inhibitor complexes.
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Authors
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J.B.Cooper,
S.I.Foundling,
T.L.Blundell,
J.Boger,
R.A.Jupp,
J.Kay.
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Ref.
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Biochemistry, 1989,
28,
8596-8603.
[DOI no: ]
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PubMed id
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Abstract
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The conformation of a statine-containing renin inhibitor complexed with the
aspartic proteinase from the fungus Endothia parasitica (EC 3.4.23.6) has been
determined by X-ray diffraction at 2.2-A resolution (R = 0.17). We describe the
structure of the complex at high resolution and compare this with a 3.0-A
resolution analysis of a bound inhibitor, L-364,099, containing a
cyclohexylalanine analogue of statine. The inhibitors bind in extended
conformations in the long active-site cleft, and the hydroxyl of the
transition-state analogue, statine, interacts strongly with the catalytic
aspartates via hydrogen bonds to the essential carboxyl groups. This work
provides a detailed structural analysis of the role of statine in peptide
inhibitors. It shows conclusively that statine should be considered a dipeptide
analogue (occupying P1 to P1') despite lacking the equivalent of a P1' side
chain, although other inhibitor residues (especially P2) may compensate by
interacting at the unoccupied S1' specificity subsite.
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Secondary reference #1
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Title
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The active site of aspartic proteinases.
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Authors
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L.Pearl,
T.Blundell.
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Ref.
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Febs Lett, 1984,
174,
96.
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PubMed id
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Secondary reference #2
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Title
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Active site of acid proteinases
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Authors
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T.L.Blundell,
H.B.Jones,
G.Khan,
G.Taylor,
T.S.Sewell,
L.H.Pearl,
S.P.Wood.
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Ref.
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proc febs meet, 1979,
60,
281.
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Secondary reference #3
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Title
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The three-Dimensional structure of acid proteinases
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Authors
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T.L.Blundell,
J.A.Jenkins,
G.Khan,
P.Roy Chowdhury,
T.Sewell,
I.J.Tickle,
E.A.Wood.
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Ref.
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proc febs meet, 1979,
52,
81.
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Secondary reference #4
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Title
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Four-Fold structural repeat in the acid proteases.
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Authors
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T.L.Blundell,
B.T.Sewell,
A.D.Mclachlan.
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Ref.
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Biochim Biophys Acta, 1979,
580,
24-31.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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Structural evidence for gene duplication in the evolution of the acid proteases.
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Authors
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J.Tang,
M.N.James,
I.N.Hsu,
J.A.Jenkins,
T.L.Blundell.
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Ref.
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Nature, 1978,
271,
618-621.
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PubMed id
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Secondary reference #6
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Title
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Homology among acid proteases: comparison of crystal structures at 3a resolution of acid proteases from rhizopus chinensis and endothia parasitica.
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Authors
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E.Subramanian,
I.D.Swan,
M.Liu,
D.R.Davies,
J.A.Jenkins,
I.J.Tickle,
T.L.Blundell.
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Ref.
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Proc Natl Acad Sci U S A, 1977,
74,
556-559.
[DOI no: ]
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PubMed id
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Secondary reference #7
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Title
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X-Ray analysis and circular dichroism of the acid protease from endothia parasitica and chymosin.
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Authors
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J.Jenkins,
I.Tickle,
T.Sewell,
L.Ungaretti,
A.Wollmer,
T.Blundell.
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Ref.
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Adv Exp Med Biol, 1977,
95,
43-60.
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PubMed id
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