Structure and order of the protein and carbohydrate domains of prothrombin fragment 1

FEBS Letters

Harlos, K.²  Holland, S.K.²  Blake, C.C.F.²  Esnouf, M.P.¹  Boys, C.W.G.² 

[1] Nuffield Department of Clinical Biochemistry, Radcliffe Infirmary, Oxford OX2 6HE, England;Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU England

关键词: Prothrombin fragment 1;    Kringle;    Carbohydrate structure;    Protein crystallography;   

DOI  :  10.1016/0014-5793(87)80429-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown