1e04
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PLASMA BETA ANTITHROMBIN-III
OverviewOverview
The crystal structure of a dimeric form of intact antithrombin has been, solved to 2.6 A, representing the highest-resolution structure of an, active, inhibitory serpin to date. The crystals were grown under, microgravity conditions on Space Shuttle mission STS-67. The overall, confidence in the structure, determined earlier from lower resolution, data, is increased and new insights into the structure-function, relationship are gained. Clear and continuous electron density is present, for the reactive centre loop region P12 to P14 inserting into the top of, the A-beta-sheet. Areas of the extended amino terminus, unique to, antithrombin and important in the binding of the glycosaminoglycan, heparin, can now be traced further than in the earlier structures. As in, the earlier studies, the crystals contain one active and one latent, molecule per asymmetric unit. Better definition of the electron density, surrounding the D-helix and of the residues implicated in the binding of, the heparin pentasaccharide (Arg47, Lys114, Lys125, Arg129) provides an, insight into the change of affinity of binding that accompanies the change, in conformation. In particular, the observed hydrogen bonding of these, residues to the body of the molecule in the latent form explains the, mechanism for the release of newly formed antithrombin-protease complexes, into the circulation for catabolic removal.
About this StructureAbout this Structure
1E04 is a Single protein structure of sequence from Homo sapiens with MAN, PO4 and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site., Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR, J Mol Biol. 1997 Feb 28;266(3):601-9. PMID:9067613
Page seeded by OCA on Mon Nov 12 16:37:59 2007