ArticleBMC biochemistry2007
The N-terminal domain of apolipoprotein B-100: structural characterization by homology modeling.
Article in BMC biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Article
- Conformation and stability properties of B17: II. Analytical investigations using differential scanning calorimetry.European biophysics journal : EBJ · 2013Article
- Low-density lipoprotein modified by myeloperoxidase in inflammatory pathways and clinical studies.Mediators of inflammation · 2013Review
- Conformation and stability properties of B17: I. Analytical investigations using circular dichroism.European biophysics journal : EBJ · 2012Article
- Effect of Structural Changes in Proteins Derived from GATA4 Nonsynonymous Single Nucleotide Polymorphisms in Congenital Heart Disease.Indian journal of pharmaceutical sciencesArticle
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Authors and funding
2 authors.
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Abstract
backgroundApolipoprotein 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.
resultsThe 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.
conclusionThe 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.
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