Summary for 1M1J
Entry DOI | 10.2210/pdb1m1j/pdb |
Related | 1EI3 1FZC |
Descriptor | Fibrinogen alpha subunit, Fibrinogen beta chain, Fibrinogen gamma chain, ... (8 entities in total) |
Functional Keywords | coiled coils, disulfide rings, fibrinogen, blood clotting |
Biological source | Gallus gallus (chicken) More |
Total number of polymer chains | 10 |
Total formula weight | 311778.33 |
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 citation | Yang, 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: 11601975DOI: 10.1021/bi011394p PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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