Structural determination of lipid-bound human blood coagulation factor IX

S. Stoylova, E. Gray, T. W. Barrowcliffe, G. Kemball-Cook, A. Holzenburg

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Human coagulation factor IX (FIX) is a serine protease which binds to a negatively charged phospholipid surface in the presence of Ca ions (Ca2+). FIX two-dimensional (2-D) crystals were obtained by the lipid layer crystallisation technique under near physiological conditions. The 2-D projection map of the protein was calculated to a resolution of 3 nm using electron crystallographic analysis. The structural organisation of membrane-bound FIX is discussed and compared with the known X-ray crystallographic data.

Original languageEnglish (US)
Pages (from-to)175-178
Number of pages4
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1383
Issue number2
DOIs
StatePublished - Apr 2 1998
Externally publishedYes

Fingerprint

Factor IX
Lipids
Serine Proteases
Crystallization
Phospholipids
X-Rays
Electrons
Ions
Membranes
X rays
Crystals
Proteins

Keywords

  • Human blood coagulation factor IX
  • Lipid-protein interaction
  • Macromolecular organisation
  • Membrane binding
  • Transmission electron microscopy and crystallography
  • Two-dimensional crystallization

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Structural determination of lipid-bound human blood coagulation factor IX. / Stoylova, S.; Gray, E.; Barrowcliffe, T. W.; Kemball-Cook, G.; Holzenburg, A.

In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1383, No. 2, 02.04.1998, p. 175-178.

Research output: Contribution to journalArticle

Stoylova, S. ; Gray, E. ; Barrowcliffe, T. W. ; Kemball-Cook, G. ; Holzenburg, A. / Structural determination of lipid-bound human blood coagulation factor IX. In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1998 ; Vol. 1383, No. 2. pp. 175-178.
@article{21b509c861734ad88ca7da827f811acb,
title = "Structural determination of lipid-bound human blood coagulation factor IX",
abstract = "Human coagulation factor IX (FIX) is a serine protease which binds to a negatively charged phospholipid surface in the presence of Ca ions (Ca2+). FIX two-dimensional (2-D) crystals were obtained by the lipid layer crystallisation technique under near physiological conditions. The 2-D projection map of the protein was calculated to a resolution of 3 nm using electron crystallographic analysis. The structural organisation of membrane-bound FIX is discussed and compared with the known X-ray crystallographic data.",
keywords = "Human blood coagulation factor IX, Lipid-protein interaction, Macromolecular organisation, Membrane binding, Transmission electron microscopy and crystallography, Two-dimensional crystallization",
author = "S. Stoylova and E. Gray and Barrowcliffe, {T. W.} and G. Kemball-Cook and A. Holzenburg",
year = "1998",
month = "4",
day = "2",
doi = "10.1016/S0167-4838(97)00219-7",
language = "English (US)",
volume = "1383",
pages = "175--178",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Structural determination of lipid-bound human blood coagulation factor IX

AU - Stoylova, S.

AU - Gray, E.

AU - Barrowcliffe, T. W.

AU - Kemball-Cook, G.

AU - Holzenburg, A.

PY - 1998/4/2

Y1 - 1998/4/2

N2 - Human coagulation factor IX (FIX) is a serine protease which binds to a negatively charged phospholipid surface in the presence of Ca ions (Ca2+). FIX two-dimensional (2-D) crystals were obtained by the lipid layer crystallisation technique under near physiological conditions. The 2-D projection map of the protein was calculated to a resolution of 3 nm using electron crystallographic analysis. The structural organisation of membrane-bound FIX is discussed and compared with the known X-ray crystallographic data.

AB - Human coagulation factor IX (FIX) is a serine protease which binds to a negatively charged phospholipid surface in the presence of Ca ions (Ca2+). FIX two-dimensional (2-D) crystals were obtained by the lipid layer crystallisation technique under near physiological conditions. The 2-D projection map of the protein was calculated to a resolution of 3 nm using electron crystallographic analysis. The structural organisation of membrane-bound FIX is discussed and compared with the known X-ray crystallographic data.

KW - Human blood coagulation factor IX

KW - Lipid-protein interaction

KW - Macromolecular organisation

KW - Membrane binding

KW - Transmission electron microscopy and crystallography

KW - Two-dimensional crystallization

UR - http://www.scopus.com/inward/record.url?scp=0037482537&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037482537&partnerID=8YFLogxK

U2 - 10.1016/S0167-4838(97)00219-7

DO - 10.1016/S0167-4838(97)00219-7

M3 - Article

VL - 1383

SP - 175

EP - 178

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -