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PDBsum entry 1flh
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.23.1
- pepsin A.
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Reaction:
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Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|- Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|- Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
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DOI no:
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Acta Crystallogr D Biol Crystallogr
57:1560-1570
(2001)
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PubMed id:
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Structure of human uropepsin at 2.45 A resolution.
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F.Canduri,
L.G.Teodoro,
V.Fadel,
C.C.Lorenzi,
V.Hial,
R.A.Gomes,
J.R.Neto,
W.F.de Azevedo.
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ABSTRACT
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The molecular structure of human uropepsin, an aspartic proteinase from the
urine produced in the form of pepsinogen A in the gastric mucosa, has been
determined by molecular replacement using human pepsin as the search model.
Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a =
50.99, b = 75.56, c = 89.90 A. Crystallographic refinement led to an R factor of
0.161 at 2.45 A resolution. The positions of 2437 non-H protein atoms in 326
residues have been determined and the model contains 143 water molecules. The
structure is bilobal, consisting of two predominantly beta-sheet lobes which, as
observed in other aspartic proteinases, are related by a pseudo-twofold axis. A
model of the uropepsin-pepstatin complex has been constructed based on the
high-resolution crystal structure of pepsin complexed with pepstatin.
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Selected figure(s)
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Figure 3.
Figure 3 Electron-density map (2F[obs] - F[calc], 1  cutoff)
of the active site of the human uropepsin showing aspartic acid
residues 32 and 215.
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Figure 5.
Figure 5 Ribbon diagram of the human uropepsin generated by
Molscript (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst.
24, 946-950.]; Merritt & Murphy, 1994[Merritt, E. A. & Murphy,
M. E. P. (1994). Acta Cryst. D50, 869-873.]) and Raster3D
(Merritt & Murphy, 1994[Merritt, E. A. & Murphy, M. E. P.
(1994). Acta Cryst. D50, 869-873.]). The three domains of
uropepsin can be observed: the C-terminal domain is in green,
the central domain is in red and the N-terminal domain is in
cyan.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
1560-1570)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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G.B.Barcellos,
R.A.Caceres,
and
W.F.de Azevedo
(2009).
Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP.
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J Mol Model,
15,
147-155.
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H.Ihara,
T.Matsumoto,
Y.Morita,
A.Hirano,
M.Okada,
N.Hashizume,
I.Shioji,
and
H.Yoshimura
(2007).
Diurnal variation of biopyrrin excretion in random urine specimens is not corrected by creatinine.
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J Clin Lab Anal,
21,
1-6.
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K.K.Manhani,
H.A.Arcuri,
N.J.da Silveira,
H.B.Uchôa,
W.F.de Azevedo,
and
F.Canduri
(2005).
Molecular models of protein kinase 6 from Plasmodium falciparum.
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J Mol Model,
12,
42-48.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
