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PDBsum entry 1bml
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Blood clotting
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PDB id
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1bml
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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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Crystal structure of the catalytic domain of human plasmin complexed with streptokinase.
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Authors
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X.Wang,
X.Lin,
J.A.Loy,
J.Tang,
X.C.Zhang.
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Ref.
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Science, 1998,
281,
1662-1665.
[DOI no: ]
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PubMed id
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Abstract
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Streptokinase is a plasminogen activator widely used in treating blood-clotting
disorders. Complexes of streptokinase with human plasminogen can hydrolytically
activate other plasminogen molecules to plasmin, which then dissolves blood
clots. A similar binding activation mechanism also occurs in some key steps of
blood coagulation. The crystal structure of streptokinase complexed with the
catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal
domain of streptokinase in the complex is hypothesized to enhance the substrate
recognition. The carboxyl-terminal domain of streptokinase, which binds near the
activation loop of plasminogen, is likely responsible for the contact activation
of plasminogen in the complex.
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Figure 1.
Fig. 1. Stereoview of the crystal structure of human
µPm-SK complex in C[  ]traces.
The µPm molecule is shown in blue with the NH[2]-terminal
short peptide in dark blue. The  ,  , and  domains
of SK are shown in yellow, green, and purple, respectively. The
chymotrypsin equivalences of the labeled µPm residues are
15 (561 in Pm), 16 (562), 57 (603), 102 (646), and 195 (741).
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Figure 2.
Fig. 2. Interactions between human µPm and the (A) and (B)
domains
of SK. µPm is shown in blue and SK in orange. The side
chains involved in the interactions are also shown as stick
models and labeled. Also labeled are the secondary structures in
the SK and domains.
Abbreviations for the amino acid residues are as follows: A,
Ala; D, Asp; E, Glu; F, Phe; H, His; K, Lys; L, Leu; N, Asn; P,
Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1998,
281,
1662-1665)
copyright 1998.
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