The N-terminal domain of apolipoprotein B-100: Structural characterization by homology modeling

Hassan Al-Ali, Hassan M. Khachfe

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Background. Apolipoprotein B-100 (apo B-100) stands as one of the largest proteins in humans. Its large size of 4536 amino acids hampers the production of X-ray diffraction quality crystals and hinders in-solution NMR analysis, and thus necessitates a domain-based approach for the structural characterization of the multi-domain full-length apo B. Results. The structure of apo B-17 (the N-terminal 17% of apolipoprotein B-100) was predicted by homology modeling based on the structure of the N-terminal domain of lipovitellin (LV), a protein that shares not only sequence similarity with B17, but also a functional aspect of lipid binding and transport. The model structure was first induced to accommodate the six disulfide bonds found in that region, and then optimized using simulated annealing. Conclusion. The content of secondary structural elements in this model structure correlates well with the reported data from other biophysical probes. The overall topology of the model conforms with the structural outline corresponding to the apo B-17 domain as seen in the EM representation of the complete LDL structure.

Original languageEnglish (US)
Article number12
JournalBMC Biochemistry
Volume8
DOIs
StatePublished - Aug 14 2007
Externally publishedYes

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Apolipoprotein B-100
Model structures
Apolipoproteins B
Simulated annealing
X-Ray Diffraction
Disulfides
Proteins
Nuclear magnetic resonance
Topology
Lipids
Amino Acids
X ray diffraction
Crystals
apolipoprotein b-17
lipovitellin
oxidized low density lipoprotein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

The N-terminal domain of apolipoprotein B-100 : Structural characterization by homology modeling. / Al-Ali, Hassan; Khachfe, Hassan M.

In: BMC Biochemistry, Vol. 8, 12, 14.08.2007.

Research output: Contribution to journalArticle

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