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PDBsum entry 1iqj
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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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Factor xa specific inhibitor that induces the novel binding model in complex with human fxa
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Authors
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T.Matsusue,
I.Shiromizu,
A.Okamoto,
K.Nakayama,
H.Nishida,
T.Mukaihira,
Y.Miyazaki,
F.Saitou,
H.Morishita,
S.Ohnishi,
H.Mochizuki.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Structure of human des(1-45) factor xa at 2.2 a resolution.
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Authors
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K.Padmanabhan,
K.P.Padmanabhan,
A.Tulinsky,
C.H.Park,
W.Bode,
R.Huber,
D.T.Blankenship,
A.D.Cardin,
W.Kisiel.
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Ref.
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J Mol Biol, 1993,
232,
947-966.
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PubMed id
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Secondary reference #2
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Title
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X-Ray structure of active site-Inhibited clotting factor xa. Implications for drug design and substrate recognition.
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Authors
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H.Brandstetter,
A.Kühne,
W.Bode,
R.Huber,
W.Von der saal,
K.Wirthensohn,
R.A.Engh.
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Ref.
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J Biol Chem, 1996,
271,
29988-29992.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Chemical formula of the DX-9065a inhibitor:
(2S)-{4-[1-acetimidoyl-(3S)-pyrrolidinyl]-oxyphenyl}-3-(7-amidino-2-naphthyl)propionic^
acid hydrochloride pentahydrate.
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Figure 3.
Fig. 3. Binding interactions of DX-9065a with fXa. The C^
 plot
and side chains involved in inhibitor binding of DX-9065a-bound^
fXa (yellow) are superimposed with the corresponding atoms of^
arginine-bound fXa (turquoise). The ligand-induced structural
changes at the S1-binding site may be seen at the side chain of^
Asp-189 and along the main chain at Gln-192. The hydrophobic
sleeve^ at the aryl-binding site (S4) is also apparent, with the
cation hole formed by Glu-97 and the carbonyl oxygens of Glu-97
and Lys-96^ at the back.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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Secondary reference #3
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Title
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Autoproteolysis or plasmin-Mediated cleavage of factor xaalpha exposes a plasminogen binding site and inhibits coagulation.
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Authors
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E.L.Pryzdial,
G.E.Kessler.
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Ref.
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J Biol Chem, 1996,
271,
16614-16620.
[DOI no: ]
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PubMed id
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Figure 4.
Fig. 4. Disulfide-linked subunit composition of
plasmin-cleaved FXa  . The
nonreduced SDS-PAGE (12% acrylamide) pattern of FXa (7
µM) digested with plasmin (0.1 µM) for 30 min was
excised and electrophoresed in a second dimension under reducing
conditions (14% acrylamide). Panel A, FXa digested
with plasmin in the presence of PCPS (300 µM) and Ca^2+ (2
mM); panel B, FXa digested
with plasmin in the presence of PCPS and EDTA (5 mM).
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Figure 7.
Fig. 7. Effect of plasmin on FXa enzymatic
activity. FXa was
subjected to autoproteolysis (  ) or
cleavage by plasmin in the presence of PCPS and Ca^2+ (  ) or PCPS
and EDTA (  ) under the
conditions described in the legend to Fig. 3. At the times
indicated, FXa enzymatic activity was evaluated by a chromogenic
substrate assay (panel A, n = 3 ± S.D.) or in a one-stage
clotting assay (panel B, n = 2 ± S.E.), as described
under ``Experimental Procedures.''
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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