Premium
Structure and order of the protein and carbohydrate domains of prothrombin fragment 1
Author(s) -
Harlos K.,
Boys C.W.G.,
Holland S.K.,
Esnouf M.P.,
Blake C.C.F.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80429-5
Subject(s) - fragment (logic) , carbohydrate , chemistry , biochemistry , order (exchange) , mathematics , business , algorithm , finance
The three‐dimensional structure of prothrombin fragment 1 has been determined by X‐ray crystallography at 3.8 Å 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 γ‐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.