1tap
From Proteopedia
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NMR SOLUTION STRUCTURE OF RECOMBINANT TICK ANTICOAGULANT PROTEIN (RTAP), A FACTOR XA INHIBITOR FROM THE TICK ORNITHODOROS MOUBATA
Overview
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.
About this Structure
1TAP is a Single protein structure of sequence from Ornithodoros moubata. Full crystallographic information is available from OCA.
Reference
NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata., Antuch W, Guntert P, Billeter M, Hawthorne T, Grossenbacher H, Wuthrich K, FEBS Lett. 1994 Sep 26;352(2):251-7. PMID:7925983
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