By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Life Science Research is now available. According to news reporting originating in Beijing, People's Republic of China, by NewsRx journalists, research stated, "Human dihydrofolate reductase-like 1 (DHFRL1) has been identified as a second human dihydrofolate reductase (DHFR) enzyme. Although DHFRL1 have high sequence homology with human DHFR, dihydrofolate (DHF) exhibits a lowered binding affinity to DHFRL1 and the corresponding molecular mechanism is still unknown."
The news reporters obtained a quote from the research from the College of Chemistry and Chemical Engineering, "To address this question, we studied the binding of DHF to DHFRL1 and DHFR by using molecular dynamics simulation. Moreover, to investigate the role the 24th residue of DHFR/DHFRL1 plays in DHF binding, R24W DHFRL1 mutant was also studied. The van der Waals interaction are more crucial for the total DHF binding energies, while the difference between the DHF binding energies of human DHFR and DHFRL1 can be attributed to the electrostatic interaction and the polar desolvation free energy. More specifically, lower DHF affinity to DHFRL1 can be mainly attributed to the reduction of net electrostatic interactions of residues Arg32 and Gln35 of DHFRL1 with DHF as being affected by Arg24. The side chain of Arg24 in DHFRL1 can extend deeply into the binding sites of DHF and NADPH, and disturb the DHF binding by steric effect, which rarely happens in human DHFR and R24W DHFRL1 mutant. Additionally, the conformation of loop I in DHFRL1 was also studied in this work. Interestingly, the loop conformation resemble to normal closed state of Escherichia coli DHFR other than the closed state of human DHFR."
According to the news reporters, the research concluded: "We hope this work will be useful to understand the general characteristics of DHFRL1."
For more information on this research see: Insight into the molecular mechanism about lowered dihydrofolate binding affinity to dihydrofolate reductase-like 1 (DHFRL1). Journal of Molecular Modeling, 2013;19(12):5187-5198. Journal of Molecular Modeling can be contacted at: Springer, 233 Spring St, New York, NY 10013, USA. (Springer - www.springer.com; Journal of Molecular Modeling - www.springerlink.com/content/1610-2940/)
Our news correspondents report that additional information may be obtained by contacting J. Gao, Univ Chinese Academy Sci, Coll Chem & Chem Engn, Beijing 100049, People's Republic of China. Additional authors for this research include W. Cui, Y.G. Du and M.J. Ji (see also Life Science Research).
Keywords for this news article include: Asia, Beijing, Reductase, Enzymes and Coenzymes, Life Science Research, People's Republic of China
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