Homology modeling and molecular dynamics simulation of human prothrombin fragment 1.
Protein Sci
; 4(11): 2341-8, 1995 Nov.
Article
in En
| MEDLINE
| ID: mdl-8563631
ABSTRACT
The crystallographic structure of bovine prothrombin fragment 1 bound with calcium ions was used to construct the corresponding human prothrombin structure (hf1/Ca). The model structure was refined by molecular dynamics to estimate the average solution structure. Accommodation of long-range ionic forces was essential to reach a stable solution structure. The gamma-carboxyglutamic acid (Gla) domain and the kringle domain of hf1/Ca independently equilibrated. Likewise, the hydrogen bond network and the calcium ion coordinations were well preserved. A discussion of the phospholipid binding of the vitamin K-dependent coagulation proteins in the context of the structure and mutational data of the Gla domain is presented.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptide Fragments
/
Protein Precursors
/
Prothrombin
/
Models, Molecular
/
Sequence Homology
Type of study:
Prognostic_studies
Limits:
Animals
/
Humans
Language:
En
Journal:
Protein Sci
Journal subject:
BIOQUIMICA
Year:
1995
Document type:
Article
Affiliation country:
United States