1m1j

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spinqualitylabelsall models 1m1j, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of native chicken fibrinogen with two different bound ligands

Overview

The crystal structure of native chicken fibrinogen (320 kDa) complexed, with two synthetic peptides has been determined at a resolution of 2.7 A., The structure provides the first atomic-resolution view of the polypeptide, chain arrangement in the central domain where the two halves of the, molecule are joined, as well as of a putative thrombin-binding site. The, amino-terminal segments of the alpha and beta chains, including, fibrinopeptides A and B, are not visible in electron density maps, however, and must be highly disordered. The alphaC domain is also very, disordered. A residue by residue analysis of the coiled coils with regard, to temperature factor shows a strong correlation between mobility and, plasmin attack sites. It is concluded that structural flexibility is an, inherent feature of fibrinogen that plays a key role in both its, conversion to fibrin and its subsequent destruction by plasmin.

About this Structure

1M1J is a Protein complex structure of sequences from Gallus gallus with NDG, NAG and CA as ligands. This structure superseeds the now removed PDB entry 1JFE. The following page contains interesting information on the relation of 1M1J with [Fibrin]. Full crystallographic information is available from OCA.

Reference

Crystal structure of native chicken fibrinogen at 2.7 A resolution., Yang Z, Kollman JM, Pandi L, Doolittle RF, Biochemistry. 2001 Oct 23;40(42):12515-23. PMID:11601975

Page seeded by OCA on Sun Nov 18 09:03:31 2007