1999
DOI: 10.1016/s0006-3495(99)76875-x
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Abstract: The crystallographic structure of human coagulation factor VIIa/tissue factor complex bound with calcium ions was used to model the solution structure of the light chain of factor VIIa (residues 1-142) in the absence of tissue factor. The Amber force field in conjunction with the particle mesh Ewald summation method to accommodate long-range electrostatic interactions was used in the trajectory calculations. The estimated TF-free solution structure was then compared with the crystal structure of factor VIIa/ti… Show more

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Cited by 13 publications
(14 citation statements)
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“…42 We found that the light chain of FVIIa, in the absence of TF, is in an extended conformation similar to the X-ray crystal structure of TF-bound FVIIa. The removal of the calcium ion bound to the EGF1 domain led to only minor structural changes within the EGF1 domain, but resulted in a substantial relative reorientation of the Gla-EGF1 domains.…”
Section: The Light Chainsupporting
confidence: 70%
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“…42 We found that the light chain of FVIIa, in the absence of TF, is in an extended conformation similar to the X-ray crystal structure of TF-bound FVIIa. The removal of the calcium ion bound to the EGF1 domain led to only minor structural changes within the EGF1 domain, but resulted in a substantial relative reorientation of the Gla-EGF1 domains.…”
Section: The Light Chainsupporting
confidence: 70%
“…Because the TF bound X-ray structure of Banner et al 33 was used to create our initial model, and because this is the only structure in which the X-ray intensities were found for all FVIIa residues (with the exception of residues 143-152 in the C-terminus of the light chain), we employ this structure as the primary reference for the majority of our structure comparisons. In the following discussion, we present a brief description of the stability of our equilibrated model system, a summary of the properties of the zymogen light chain (with a comparison to our previous simulation 42 in which only the light chain of FVII was used), and a detailed comparison of the zymogen SP domain with that of the activated form evaluated from X-ray crystal structures. Also, we will briefly discuss the possible function of TF interactions.…”
Section: Resultsmentioning
confidence: 99%
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