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PDBsum entry 2er6
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Hydrolase/hydrolase inhibitor
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PDB id
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2er6
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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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The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
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Authors
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J.Cooper,
S.Foundling,
A.Hemmings,
T.Blundell,
D.M.Jones,
A.Hallett,
M.Szelke.
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Ref.
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Eur J Biochem, 1987,
169,
215-221.
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PubMed id
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Abstract
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The conformation of a synthetic polypeptide inhibitor, bound to the active site
of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been
determined by X-ray diffraction at 0.20-nm resolution and refined to an
agreement factor of 0.20. The inhibitor: Pro Thr Glu Phe-R-Phe Arg Glu (R =
-CH2NH-) is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in
place of the scissile bond, a reduced peptide group which is resistant to
hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in
an extended conformation with the reduced bond close to the essential aspartate
side-chains of the enzyme. The hydrogen bonds and hydrophobic interactions
between the enzyme and the inhibitor do not induce large conformational changes.
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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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