Seshadri K, Balaji P V, Rao V S, Vishveshwara S
Molecular Biophysics Unit, Indian Institute of Science, Bangalore.
J Biomol Struct Dyn. 1993 Oct;11(2):395-415. doi: 10.1080/07391102.1993.10508734.
Different modes of binding of pyrimidine monophosphates 2'-UMP, 3'-UMP, 2'-CMP and 3'-CMP to ribonuclease (RNase) A are studied by energy minimization in torsion angle and subsequently in Cartesian coordinate space. The results are analysed in the light of primary binding sites. The hydrogen bonding pattern brings out roles for amino acids such as Asn44 and Ser123 apart from the well known active site residues viz., His12,Lys41,Thr45 and His119. Amino acid segments 43-45 and 119-121 seem to be guiding the ligand binding by forming a pocket. Many of the active site charged residues display considerable movement upon nucleotide binding.
通过在扭转角以及随后在笛卡尔坐标空间中进行能量最小化，研究了嘧啶单磷酸酯2'-UMP、3'-UMP、2'-CMP和3'-CMP与核糖核酸酶（RNase）A的不同结合模式。根据主要结合位点对结果进行分析。除了众所周知的活性位点残基，即His12、Lys41、Thr45和His119外，氢键模式还揭示了Asn44和Ser123等氨基酸的作用。氨基酸片段43 - 45和119 - 121似乎通过形成一个口袋来引导配体结合。许多活性位点带电荷的残基在核苷酸结合后会发生相当大的移动。
