1tcp
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tcp OCA], [http://www.ebi.ac.uk/pdbsum/1tcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tcp RCSB]</span> | ||
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[[Category: factor xa serine protease inhibitor]] | [[Category: factor xa serine protease inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:18 2008'' |
Revision as of 20:54, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE DETERMINATION OF TICK ANTICOAGULANT PEPTIDE (TAP)
Overview
Tick anticoagulant peptide (TAP) is a potent and selective 60-amino acid inhibitor of the serine protease Factor Xa (fXa), the penultimate enzyme in the blood coagulation cascade. The structural features of TAP responsible for its remarkable specificity for fXa are unknown, but the binding to its target appears to be unique. The elucidation of the TAP structure may facilitate our understanding of this new mode of serine protease inhibition and could provide a basis for the design of novel fXa inhibitors. Analyses of homo- and heteronuclear two-dimensional NMR spectra (total correlation spectroscopy, nuclear Overhauser effect spectroscopy [NOESY], constant time heteronuclear single quantum correlation spectroscopy [CT-HSQC], and HSQC-NOESY; 600 MHz; 1.5 mM TAP; pH 2.5) of unlabeled, 13C-labeled, and 15N-labeled TAP provided nearly complete 1H sequence-specific resonance assignments. Secondary structural elements were identified by characteristic NOE patterns and D2O amide proton-exchange experiments. A three-dimensional structure of TAP was generated from 412 NOESY-derived distance and 47 dihedral angle constraints. The structural elements of TAP are similar in some respects to those of the Kunitz serine protease inhibitor family, with which TAP shares weak sequence homology. This structure, coupled with previous kinetic and biochemical information, confirms previous suggestions that TAP has a unique mode of binding to fXa.
About this Structure
1TCP is a Single protein structure of sequence from Ornithodoros moubata. Full crystallographic information is available from OCA.
Reference
NMR structure determination of tick anticoagulant peptide (TAP)., Lim-Wilby MS, Hallenga K, de Maeyer M, Lasters I, Vlasuk GP, Brunck TK, Protein Sci. 1995 Feb;4(2):178-86. PMID:7538849
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