Crystal structure of native chicken fibrinogen at 2.7 A resolution
| Autor: | Justin M. Kollman, Russell F. Doolittle, Leela Pandi, Zhe Yang |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Plasmin
Molecular Sequence Data Crystal structure Fibrinogen Crystallography X-Ray Biochemistry Fibrin Protein Structure Secondary Residue (chemistry) Protein structure medicine Animals Humans Amino Acid Sequence Disulfides Peptide sequence biology Sequence Homology Amino Acid Chemistry Resolution (electron density) Thrombin Lampreys Peptide Fragments Protein Structure Tertiary Crystallography biology.protein Cattle Crystallization Chickens medicine.drug Protein Binding |
| Zdroj: | Biochemistry. 40(42) |
| ISSN: | 0006-2960 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|