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1M1J

Crystal structure of native chicken fibrinogen with two different bound ligands

Replaces:  1JFE
Summary for 1M1J
Entry DOI10.2210/pdb1m1j/pdb
Related1EI3 1FZC
DescriptorFibrinogen alpha subunit, Fibrinogen beta chain, Fibrinogen gamma chain, ... (8 entities in total)
Functional Keywordscoiled coils, disulfide rings, fibrinogen, blood clotting
Biological sourceGallus gallus (chicken)
More
Total number of polymer chains10
Total formula weight311778.33
Authors
Yang, Z.,Kollman, J.M.,Pandi, L.,Doolittle, R.F. (deposition date: 2002-06-19, release date: 2002-06-26, Last modification date: 2024-10-30)
Primary citationYang, Z.,Kollman, J.M.,Pandi, L.,Doolittle, R.F.
Crystal Structure of Native Chicken Fibrinogen at 2.7 A Resolution
Biochemistry, 40:12515-12523, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11601975
DOI: 10.1021/bi011394p
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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