Details

Autor(en) / Beteiligte

• Antuch, W.
• Güntert, P.
• Billeter, M.
• Hawthorne, T.
• Grossenbacher, H.
• Wüthrich, K.

Titel

NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata

Ist Teil von

• FEBS letters, 1994-09, Vol.352 (2), p.251-257

Ort / Verlag

England: Elsevier B.V

Erscheinungsjahr

1994

Link zum Volltext

Quelle

Electronic Journals Library

Beschreibungen/Notizen

• 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°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 β-sheet with residues 22–28 and 32–38, and an α-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 β-sheet and the C-terminal α-helix as well as the N-terminal 20-residue segment preceding the β-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.