1lwu

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spinqualitylabelsall models 1lwu, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide

Overview

The crystal structure of fragment D from lamprey fibrinogen has been, determined at 2.8 A resolution. The 89 kDa protein was cocrystallized with, the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens-but not, lamprey-corresponds to the B knob exposed by thrombin. Because lamprey, fragment D is more than 50% identical in sequence with human fragment D, the structure of which has been reported previously, it was possible to, use the method of molecular replacement. The space group of the lamprey, crystals is P1; there are four molecules in the unit cell. Although the, fragments are packed head to head by the same D:D interface as is observed, in other related preparations containing fragments D, the tails are, uniquely joined by an unnatural association of the terminal sections of, the residual coiled coils from adjacent molecules. Some features of the, lamprey structure are clearer than have been observed in previous fragment, D structures, including the beta-chain carbohydrate cluster, for one, and, the important gamma-chain carboxyl-terminal segment, for another. The most, significant differences between the lamprey and human structures occur in, connecting loops at the entryways to the beta-chain and gamma-chain, binding pockets.

About this Structure

1LWU is a Protein complex structure of sequences from Petromyzon marinus with NDG, MAN, NAG, GAL, CA and NH2 as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide., Yang Z, Spraggon G, Pandi L, Everse SJ, Riley M, Doolittle RF, Biochemistry. 2002 Aug 13;41(32):10218-24. PMID:12162736

Page seeded by OCA on Tue Nov 20 20:57:07 2007