1m1j
From Proteopedia
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| , resolution 2.70Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:37:43 2008
Categories: Fibrin | Gallus gallus | Protein complex | Doolittle, R F. | Kollman, J M. | Pandi, L. | Yang, Z. | CA | NAG | NDG | Coiled coil | Disulfide ring | Fibrinogen
