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BMC Biochemistry

, 8:12

First Online: 22 July 2007Received: 09 October 2006Accepted: 22 July 2007

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.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2091-8-12 contains supplementary material, which is available to authorized users.

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Autor: Hassan Al-Ali - Hassan M Khachfe

Fuente: https://link.springer.com/article/10.1186/1471-2091-8-12



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