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Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-Å resolution
- Publication Year :
- 2001
- Publisher :
- The National Academy of Sciences, 2001.
-
Abstract
- The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E 5 fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular “handshake” by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aα and Bβ chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal γ chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two γ chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E 5 fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.
- Subjects :
- Models, Molecular
Stereochemistry
Molecular Sequence Data
Crystal structure
Crystallography, X-Ray
Fibrin
Fibrin Fibrinogen Degradation Products
chemistry.chemical_compound
Thrombin
medicine
Molecule
Animals
Amino Acid Sequence
Binding site
Peptide sequence
Multidisciplinary
biology
Chemistry
Fibrinogen
Biological Sciences
Protein Structure, Tertiary
Crystallography
Monomer
biology.protein
DNA supercoil
Cattle
Dimerization
medicine.drug
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....f88b8a7c21adb92c3429bbb1d5ae3e38