Structural Analysis of Factor IX Protein Variants to Predict Functional Aberration Causing Haemophilia B
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Structural Analysis of Factor IX Protein Variants to Predict
Functional Aberration Causing Haemophilia B
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| Creator |
Mukherjee, S
Saha, A Biswas, P Mandal, C Ray, Kunal |
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| Subject |
Molecular & Human Genetics
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| Description |
Factor IX (FIX) is a vitamin K-dependent serine
protease precursor that upon activation plays a
crucial role in blood coagulation [1]. A lack of its
coagulant activity results in haemophilia B, a bleeding
disorder affecting nearly 30 000 male births
worldwide. Human FIX is synthesized in the liver as
a precursor molecule containing 461 amino acids, of
which the first 46 residues are removed. During
biosynthesis, the protein undergoes several post posttranslational
modifications, which include c-carboxylation
and hydroxylation. The resulting mature
protein containing 415 amino acids is a zymogen of
serine protease. Upon initiation of blood coagulation,
either FVIIa or FXIa converts FIX to its active
form FIXa by proteolysis. During this process, the
activation peptide (residue 146–180) is cleaved off
resulting in a two-chain molecule comprising of
covalently linked light and heavy chains, which are
organized into several distinct domains: an aminoterminal
c-carboxyglutamic acid (Gla) domain (residues
1–40), a short hydrophobic segment (residues
41–46), two epidermal growth factor (EGF)-like
domains [EGF1 residues (47–84) and EGF2 residues
(85–127)] and a carboxyl-terminal serine protease
domain.
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| Date |
2008
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/296/1/HAEMOPHILIA%2C14(_5)%2C1076%2D1081%2C2008[41].pdf
Mukherjee, S and Saha, A and Biswas, P and Mandal, C and Ray, Kunal (2008) Structural Analysis of Factor IX Protein Variants to Predict Functional Aberration Causing Haemophilia B. Haemophilia, 14 (5). pp. 1076-1081. |
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| Relation |
http://dx.doi.org/10.1111/j.1365-2516.2008.01788.x
http://www.eprints.iicb.res.in/296/ |
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