Crystal structure of native chicken fibrinogen at 2.7 A resolution.
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.
Yang
Z
Z
Center for Molecular Genetics, University of California, San Diego, La Jolla, California 92093-0634, USA.
Kollman
J M
JM
Pandi
L
L
Doolittle
R F
RF
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002645:Chickens; D003460:Crystallization; D018360:Crystallography, X-Ray; D004220:Disulfides / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007798:Lampreys; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013917:Thrombin / Q000378:metabolism
D004220:Disulfides; D010446:Peptide Fragments; D005340:Fibrinogen; D013917:Thrombin