Changes in the Factor VIII C2 domain upon membrane binding determined by hydrogen–deuterium exchange MS

2014 ◽  
Vol 461 (3) ◽  
pp. 443-451 ◽  
Author(s):  
Dionysios Pantazatos ◽  
Christopher R. Gessner ◽  
Virgil L. Woods ◽  
Gary E. Gilbert
Keyword(s):  
Factor Viii ◽  
Blood Coagulation ◽  
Membrane Binding ◽  
Coagulation Factor ◽  
Coagulation Factor Viii ◽  
Hydrogen Deuterium Exchange ◽  
Factor Ixa ◽  
Hydrogen Deuterium ◽  
Binding Peptides ◽  
Blood Coagulation Factor Viii

Blood coagulation Factor VIII binds to a membrane in order to function as a cofactor for Factor IXa, preventing haemophilia. The present study indicates that membrane-binding peptides of Factor VIII are largely protected from water exposure, indicating that they become immersed in the membrane.

scholarly journals The 3.2 Å structure of a bioengineered variant of blood coagulation factor VIII indicates two conformations of the C2 domain

2019 ◽  
Vol 18 (1) ◽  
pp. 57-69 ◽  
Author(s):  
Ian W. Smith ◽  
Anne E. d'Aquino ◽  
Christopher W. Coyle ◽  
Andrew Fedanov ◽  
Ernest T. Parker ◽  
...  
Keyword(s):  
Factor Viii ◽  
Blood Coagulation ◽  
Coagulation Factor ◽  
Coagulation Factor Viii ◽  
C2 Domain ◽  
Blood Coagulation Factor Viii

scholarly journals Limited Promiscuity of HLA-DRB1 Presented Peptides Derived of Blood Coagulation Factor VIII

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e80239 ◽  
Author(s):  
Simon D. van Haren ◽  
Aleksandra Wroblewska ◽  
Eszter Herczenik ◽  
Paul H. Kaijen ◽  
Aleksandra Ruminska ◽  
...  
Keyword(s):  
Factor Viii ◽  
Blood Coagulation ◽  
Coagulation Factor ◽  
Coagulation Factor Viii ◽  
Blood Coagulation Factor Viii
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