2pf1
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STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION
OverviewOverview
The structure of bovine prothrombin fragment 1 has been refined at 2.25 A, resolution using high resolution measurements made with the synchrotron, beam at CHESS. The synchrotron data were collected photographically by, oscillation methods (R-merge = 0.08). These were combined with lower order, diffractometer data for refinement purposes. The structure was refined, using restrained least-squares methods with the program PROLSQ to a, crystallographic R-value of 0.175. The structure includes 105 water, molecules with occupancies of greater than 0.6. The first 35 residues, (Ala1-Leu35) of the N-terminal gamma-carboxy glutamic acid-domain, (Ala1-Cys48) of fragment 1 are disordered as are two carbohydrate chains, of Mr approximately 5000; the latter two combine to render 40% of the, structure disordered. The folding of the kringle of fragment 1 is related, to the close intramolecular contact between the inner loop disulfide, groups. Half of the conserved sequence of the kringle forms an inner core, surrounding these disulfide groups. The remainder of the sequence, conservation is associated with the many turns of the main chain. The, Pro95 residue of the kringle has a cis conformation and Tyr74 is ordered, in fragment 1, although nuclear magnetic resonance studies indicate that, the comparable residue of plasminogen kringle 4 has two positions. Surface, accessibility calculations indicate that none of the disulfide groups of, fragment 1 is accessible to solvent.
About this StructureAbout this Structure
2PF1 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of bovine prothrombin fragment 1 refined at 2.25 A resolution., Seshadri TP, Tulinsky A, Skrzypczak-Jankun E, Park CH, J Mol Biol. 1991 Jul 20;220(2):481-94. PMID:1856869
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