| First Author | Yang Z | Year | 2001 |
| Journal | Biochemistry | Volume | 40 |
| Issue | 42 | Pages | 12515-23 |
| PubMed ID | 11601975 | Mgi Jnum | J:72161 |
| Mgi Id | MGI:2151949 | Doi | 10.1021/bi011394p |
| Citation | Yang Z, et al. (2001) Crystal structure of native chicken fibrinogen at 2.7 a resolution(,). Biochemistry 40(42):12515-23 |
| abstractText | 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. |
