Deriving the generic structure of the fibronectin type II domain from the prothrombin Kringle 1 crystal structure
| Autor: | Colin C.F. Blake, Karl Harlos, S. K. Holland |
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| Jazyk: | angličtina |
| Rok vydání: | 1987 |
| Předmět: |
Models
Molecular Molecular model Stereochemistry Protein Conformation Molecular Sequence Data Sequence alignment Biology General Biochemistry Genetics and Molecular Biology Kringle domain Homology (biology) Protein structure Sequence Homology Nucleic Acid Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence General Immunology and Microbiology General Neuroscience Biological Evolution Protein tertiary structure Fibronectins Fibronectin type II domain Biochemistry Factor XII Cattle Prothrombin Research Article |
| Popis: | The proposed homology between the fibronectin type II domain and the Kringle domains of blood clotting and fibrinolytic proteins has been examined in three dimensions by substituting the type II sequence into the bovine prothrombin Kringle 1 tertiary structure, determined by X-ray crystallographical methods at 3.8 A. Structural substitution of aligned amino acids of the type II domains and the Kringle produces a compact chain fold and deletions and insertions in the type II sequence are accommodated within the modelled structure. This confirms the structural homology between the two domains and verifies the sequence alignment and common evolution of the type II and Kringle units. The two structures contain homologous hydrophobic cores, centered around the two disulphide bridges which link conserved beta-type strands. Gross differences between the two domains occur in exterior loops and potential functional sites in these regions of the type II structures as found in fibronectin, Factor XII and seminal fluid protein PDC-109 are proposed. We suggest that the domains evolved from a common ancestral protein comprising the hydrophobic core and disulphide arrangement which later diverged to bind different macromolecules through adaptation of the external loops. |
| Databáze: | OpenAIRE |
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