1m1j | pdb_00001m1j

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Crystal structure of native chicken fibrinogen with two different bound ligands

File:1m1j.gif


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1m1j, resolution 2.70Å
Ligands: NDG, NAG and CA
Coordinates: save as pdb, mmCIF, xml



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. This structure supersedes 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

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