Sandbox Reserved 194: Difference between revisions
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To determine the structural characteristics of RNA substrate binding to RNase A, X-ray crystallography was used to image inhibitory DNA tetramers bound to the enzyme. DNA lacks the 2′OH essential to RNA cleavage, making the complex more conducive to crystallography. In previous studies, <scene name='Sandbox_Reserved_194/1rta_structure/1'> | To determine the structural characteristics of RNA substrate binding to RNase A, X-ray crystallography was used to image inhibitory DNA tetramers bound to the enzyme. DNA lacks the 2′OH essential to RNA cleavage, making the complex more conducive to crystallography. In previous studies, <scene name='Sandbox_Reserved_194/1rta_structure/1'> | ||
the RNase A - thymidylic acid tetramer (d(pT)4) complex</scene> has provided information into the specificity of the binding pocket subunits, B0, B1, B2 and B3. Many interactions observed in this complex occur between amino acid residues and the nucleic acid backbone such as hydrogen bonding between the | the RNase A - thymidylic acid tetramer (d(pT)4) complex</scene> has provided information into the specificity of the binding pocket subunits, B0, B1, B2 and B3. Many interactions observed in this complex occur between amino acid residues and the nucleic acid backbone such as hydrogen bonding between the <scene name='Sandbox_Reserved_194/1rta_structure_arg/1'>T300 phosphate and Arg39</scene>. Because of the interactions with the <scene name='Sandbox_Reserved_194/1rta_structure_thr/1'>N3 of T302 and Thr45 in the B1 position</scene>, it appears this site is exclusive to pyrimidines. ‘<ref>PMID:1429575</ref>’ | ||
[[Image:1RCN_zoom.png|thumb|left|275px|ApTpApApG complexed with ribonuclease A]] | [[Image:1RCN_zoom.png|thumb|left|275px|ApTpApApG complexed with ribonuclease A]] | ||
