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Calcium binding to the first EGF-like module of human factor IX in a recombinant fragment containing residues 1-85. Mutations V46E and Q50E each manifest a negligible increase in calcium affinity

Persson, Kristina LU ; Astermark, Jan LU ; Bjork, I and Stenflo, Johan LU (1998) In FEBS Letters 421(2). p.100-104
Abstract
The first EGF-like module of human coagulation factor IX contains a single functionally important calcium ion binding site. We have now shown the dissociation constant for this site to be approximately 160 microM in a recombinant protein fragment consisting of residues 1-85 in human fIX. This represents a approximately 10-fold increase in affinity as compared with the isolated EGF module (residues 46-85). The Gla module (here with Glu instead of Gla) thus increases the affinity of the EGF module calcium ion binding site. Each of two mutations, V46E and Q50E, made to investigate whether the extra negative charge would increase the affinity of the calcium binding site manifested a negligible increase in affinity.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Site-directed mutagenesis, Human factor IX, Dissociation constant, Calcium binding, EGF-like module
in
FEBS Letters
volume
421
issue
2
pages
100 - 104
publisher
Wiley-Blackwell
external identifiers
  • pmid:9468287
  • scopus:0032498121
ISSN
1873-3468
DOI
10.1016/S0014-5793(97)01546-9
language
English
LU publication?
yes
id
82fde253-fd4f-4a2c-ae4f-e89e95d1ee4e (old id 1113645)
date added to LUP
2008-07-16 09:19:25
date last changed
2017-01-01 07:04:11
@article{82fde253-fd4f-4a2c-ae4f-e89e95d1ee4e,
  abstract     = {The first EGF-like module of human coagulation factor IX contains a single functionally important calcium ion binding site. We have now shown the dissociation constant for this site to be approximately 160 microM in a recombinant protein fragment consisting of residues 1-85 in human fIX. This represents a approximately 10-fold increase in affinity as compared with the isolated EGF module (residues 46-85). The Gla module (here with Glu instead of Gla) thus increases the affinity of the EGF module calcium ion binding site. Each of two mutations, V46E and Q50E, made to investigate whether the extra negative charge would increase the affinity of the calcium binding site manifested a negligible increase in affinity.},
  author       = {Persson, Kristina and Astermark, Jan and Bjork, I and Stenflo, Johan},
  issn         = {1873-3468},
  keyword      = {Site-directed mutagenesis,Human factor IX,Dissociation constant,Calcium binding,EGF-like module},
  language     = {eng},
  number       = {2},
  pages        = {100--104},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Calcium binding to the first EGF-like module of human factor IX in a recombinant fragment containing residues 1-85. Mutations V46E and Q50E each manifest a negligible increase in calcium affinity},
  url          = {http://dx.doi.org/10.1016/S0014-5793(97)01546-9},
  volume       = {421},
  year         = {1998},
}