Structure of tick anticoagulant peptide at 1.6 Å resolution complexed with bovine pancreatic trypsin inhibitor

The structure of tick anticoagulant peptide (TAP) has been determined by X-ray crystallography at 1.6 Å resolution complexed with bovine pancreatic trypsin inhibitor (BPTI). The TAP–BPTI crystals are tetragonal, a = b = 46.87, c = 50.35 Å, space group P41, four complexes per unit cell. The TAP molec...

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Veröffentlicht in:	Protein science 2000-02, Vol.9 (2), p.265-272
Hauptverfasser:	ST. CHARLES, ROBERT, PADMANABHAN, K., ARNI, R.V., PADMANABHAN, K.P., TULINSKY, A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Aprotinin - chemistry Aprotinin - genetics Arthropod Proteins bovine pancreatic trypsin inhibitor Cattle conformational changes Crystallography, X-Ray factor Xa Factor Xa Inhibitors Hydrogen Bonding In Vitro Techniques Macromolecular Substances Molecular Sequence Data Peptides - chemistry Peptides - genetics Protein Conformation Static Electricity tick anticoagulant peptide Ticks
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