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PDBsum entry 1tap
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Proteinase inhibitor
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PDB id
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1tap
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References listed in PDB file
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Key reference
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Title
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Nmr solution structure of the recombinant tick anticoagulant protein (rtap), A factor xa inhibitor from the tick ornithodoros moubata.
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Authors
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W.Antuch,
P.Güntert,
M.Billeter,
T.Hawthorne,
H.Grossenbacher,
K.Wüthrich.
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Ref.
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FEBS Lett, 1994,
352,
251-257.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of the recombinant tick anticoagulant protein (rTAP) was
determined by 1H nuclear magnetic resonance (NMR) spectroscopy in aqueous
solution at pH 3.6 and 36 degrees C. rTAP is a 60-residue protein functioning as
a highly specific inhibitor of the coagulation protease factor Xa, which was
originally isolated from the tick Ornithodoros moubata. Its regular secondary
structure consists of a two-stranded antiparallel beta-sheet with residues 22-28
and 32-38, and an alpha-helix with residues 51-60. The relative orientation of
these regular secondary structure elements has nearly identical counterparts in
the bovine pancreatic trypsin inhibitor (BPTI). In contrast, the loop between
the beta-sheet and the C-terminal alpha-helix as well as the N-terminal
20-residue segment preceding the beta-sheet adopt different three-dimensional
folds in the two proteins. These observations are discussed with regard to the
implication of different mechanisms of protease inhibition by rTAP and by
Kunitz-type protein proteinase inhibitors.
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Secondary reference #1
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Title
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Tick anticoagulant peptide (tap) is a novel inhibitor of blood coagulation factor xa.
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Authors
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L.Waxman,
D.E.Smith,
K.E.Arcuri,
G.P.Vlasuk.
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Ref.
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Science, 1990,
248,
593-596.
[DOI no: ]
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PubMed id
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