Structure and order of the protein and carbohydrate domains of prothrombin fragment 1.
The three-dimensional structure of prothrombin fragment 1 has been determined by X-ray crystallography at 3.8 A resolution. The fragment is composed of a number of structural units, some of which are ordered while others are disordered. The ordered part of the structure includes a compact kringle unit, a helical domain and a carbohydrate chain. The kringle structure is organized around a close pair of buried disulfide bridges. One of its carbohydrate chains, that attached to Asn 101, is fully ordered, but the carbohydrate chain attached to Asn 77 appears to be disordered. The calcium binding unit is composed of a disordered part containing all ten gamma-carboxyglutamic acid residues and an ordered part forming the helical domain. The highly conserved residues Phe 41, Trp 42 and Tyr 45, which form a hydrophobic cluster on the first helix, interact around a crystallographic two-fold axis with the equivalent residues in another molecule to form a dimer in the crystal.
Harlos
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K
Laboratory of Molecular Biophysics, University of Oxford, England.
Boys
C W
CW
Holland
S K
SK
Esnouf
M P
MP
Blake
C C
CC
D000595:Amino Acid Sequence; D002236:Carbohydrate Conformation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D011498:Protein Precursors; D011516:Prothrombin; D014961:X-Ray Diffraction
D010446:Peptide Fragments; D011498:Protein Precursors; C029733:prothrombin fragment 1; D011516:Prothrombin