[Structural organization of 2C-terminal region and its analogs in a subunit of ribonucleotide reductase from herpes virus].
By means of conformational analysis, the spatial structure and conformational potential of the H-Tyr-Ala-Gly-Ala-Val-Val-Asn-Asp-Leu-OH molecule, which corresponds to sequence 329-337 of the subunit 2 C-terminal region of the herpes virus ribonucleotide reductase, were studied. It was shown that its spatial organization can be described by a set of 17 low-energy conformations of the backbone. The "reverse conformational problem" for this molecule was solved to enable the prediction of a series of synthetic analogues matching the set of low-energy, potentially physiologically active conformations.
Rasulzade State University, Baku, Azerbaijan.
N A
NA
Akhmedov
G D
GD
Abbasova
R M
RM
Abbasly
N F
NF
Akhmedov
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D018258:Herpesvirus 2, Human / Q000737:chemistry / Q000201:enzymology*; D006801:Humans; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D012264:Ribonucleotide Reductases / Q000737:chemistry*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D009842:Oligopeptides; D012264:Ribonucleotide Reductases
Strukrurnaia organizatsiia C-kontsevogo uchastka sub''edinitsy 2 ribonukleotidreduktazy virusa gerpesa i ego analogov.