Electrostatic Signatures of Adenine-and Guanine-binding Sites in Proteins
Basu Gautam
2003
Seibutsu Butsuri
Identificat ・ ion and Charactcrization of Ligand binding sites in proteins is fundamen 七 a且f ( )r understanding protein funct1on . We have ana − lyzed electrostatic potenti 誠s at ad ¢ nin ← and guaiiilsebinding sites in a nori −redundarit set of proteins wlth a view to identify consensus characteristics of the binding sites. Only a limited nunlber ofdistinct patterns ofconsensus electroStatic pQtentiaL at the binding sites were ident , ified for adeninff and gllanine −binding sit, es . This
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... cates that despite no apParent structural or sequence consensus at the binding sites , the overall effect of the protein at the binding site is conserved at the level of electrostatic potelltial distribution . The consensus pat − terns at the adeninebinding sites showed more variety than those at guanine − binding sites , Each consemsus pattern is c laracterized by its speclfic ability to bind cognate ligand and discrimlnate non − eognate lignmds , found to correlat . e with ph / sicechemlcal eonstraint imposed by the biologicaL role of the bound ligand , its biologica ユabundance and uniqueness of the entire ligand ( incLuding the non − purine part) . Struct , ural features] ike hydrogen bonds were found to eorreiate with c 〔Dnsensuhs patterns , but only for se1 [ x : t・ ed atom sites . Final] y、 based 〔 Dn the observed consertsus patterms, a simple score is pr 〔 Dp 〔 nsed and testOd successfully that can differentiate adenine and guanine − binding sites in proteins . StructurAL biology ln translatioll system of genetic code Amajor problem in biolo 爵 ・ is that the fnnctions of mQst genes re main unknown evell when there is anlpLe evoh コ t, i〔 } nary inbrmation on their sequence and structural information on their prot , ein product . W 白 will di日cuss how these distinct types of daba rr 且 ay be intugrated tQ identify canonical determina皿 ts 【 ) f structure and function . Experi − ments show that these determlnaIits ideiitify fimctional g . ites mid that they can bu manipulated predictably to a1 匕 er function a 皿 d interac − tions along the G pmtein signaling pathway 、 We will also present other results that demonstrate the scalability of this EvQiution 町
doi:10.2142/biophys.43.s3_2
fatcat:5zr5mjph5rf5flr2jvg6bjsugu