ArticleThe journal of physical chemistry. B2020
Computational Investigation of APOBEC3H Substrate Orientation and Selectivity.
Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
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2 authors.
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Abstract
APOBEC3H is a cytidine deaminase protein most well-known for its involvement in antiretroviral activity in humans. It acts upon a single stranded DNA (ssDNA) substrate with preferential targeting of a 5'-TCA-3' motif. Currently available crystal structures do not include the ssDNA substrate in the A3H system, nor is the mechanism of recognition for the preferred sequence known. To determine the position and orientation of the substrate in the active site, we used high-performance computing to perform molecular dynamics simulations on several systems of APOBEC3H. We examined different DNA sequences in the active site to determine the structural and chemical mechanism by which the preferred sequence is recognized. We found residues N49, K50, K51, and K52 to be relevant to the recognition of 3'-adenine and residues S86 and S87 to be relevant to the recognition of 5'-thymine, with both recognitions primarily driven by electrostatic nonbonded interactions.
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