Conformation of the propeptide domain of factor IX

Jya Wei Cheng; Chinpan Chen; Tai Huang Huang; Shan Ho Chou; Shi Han Chen

doi:10.1016/0304-4165(95)00080-U

Conformation of the propeptide domain of factor IX

Jya Wei Cheng^*, Chinpan Chen, Tai Huang Huang, Shan Ho Chou, Shi Han Chen

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for γ-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional ¹H-NMR and CD studies indicate that this peptide motif adopts an α-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic α-helix within the propeptide domain of factor IX could create a recognition surface for γ-carboxylase. The influences of mutations and their relationship with the α-helical structure are discussed.

Original language	English
Pages (from-to)	227-231
Number of pages	5
Journal	BBA - General Subjects
Volume	1245
Issue number	2
DOIs	https://doi.org/10.1016/0304-4165(95)00080-U
Publication status	Published - 1995 Oct 19
Externally published	Yes

Keywords

Blood clotting proteins
CD
Factor IX
Hemophilia B
NMR
Propeptide
Solution conformation

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0304-4165(95)00080-U

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title = "Conformation of the propeptide domain of factor IX",

abstract = "The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for γ-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional 1H-NMR and CD studies indicate that this peptide motif adopts an α-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic α-helix within the propeptide domain of factor IX could create a recognition surface for γ-carboxylase. The influences of mutations and their relationship with the α-helical structure are discussed.",

keywords = "Blood clotting proteins, CD, Factor IX, Hemophilia B, NMR, Propeptide, Solution conformation",

author = "Cheng, {Jya Wei} and Chinpan Chen and Huang, {Tai Huang} and Chou, {Shan Ho} and Chen, {Shi Han}",

note = "Funding Information: We would like to thank Dr. Art. R. Thompson for critical reviewing the manuscript, Dr. Ping-Chiang Lyu for fruitful discussions and Mr. C.C. Cheng for CD measurements. This work is supported in part by grants from the National Science Council, ROC (J.W.C.) and by a clinical research grant 6-463 from the March of Dimes Birth Defects fundation (S.H.C.).",

year = "1995",

month = oct,

day = "19",

doi = "10.1016/0304-4165(95)00080-U",

language = "English",

volume = "1245",

pages = "227--231",

journal = "BBA - General Subjects",

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publisher = "Elsevier",

number = "2",

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TY - JOUR

T1 - Conformation of the propeptide domain of factor IX

AU - Cheng, Jya Wei

AU - Chen, Chinpan

AU - Huang, Tai Huang

AU - Chou, Shan Ho

AU - Chen, Shi Han

N1 - Funding Information: We would like to thank Dr. Art. R. Thompson for critical reviewing the manuscript, Dr. Ping-Chiang Lyu for fruitful discussions and Mr. C.C. Cheng for CD measurements. This work is supported in part by grants from the National Science Council, ROC (J.W.C.) and by a clinical research grant 6-463 from the March of Dimes Birth Defects fundation (S.H.C.).

PY - 1995/10/19

Y1 - 1995/10/19

N2 - The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for γ-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional 1H-NMR and CD studies indicate that this peptide motif adopts an α-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic α-helix within the propeptide domain of factor IX could create a recognition surface for γ-carboxylase. The influences of mutations and their relationship with the α-helical structure are discussed.

AB - The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for γ-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional 1H-NMR and CD studies indicate that this peptide motif adopts an α-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic α-helix within the propeptide domain of factor IX could create a recognition surface for γ-carboxylase. The influences of mutations and their relationship with the α-helical structure are discussed.

KW - Blood clotting proteins

KW - CD

KW - Factor IX

KW - Hemophilia B

KW - NMR

KW - Propeptide

KW - Solution conformation

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U2 - 10.1016/0304-4165(95)00080-U

DO - 10.1016/0304-4165(95)00080-U

M3 - Article

C2 - 7492582

AN - SCOPUS:0028790066

SN - 0304-4165

VL - 1245

SP - 227

EP - 231

JO - BBA - General Subjects

JF - BBA - General Subjects

IS - 2

ER -

Conformation of the propeptide domain of factor IX

Abstract

Keywords

ASJC Scopus subject areas

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