RNase A: Difference between revisions
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[[Image:1RTAnew.png|thumb|left|200px|Thymidylic acid tetramer complexed with ribonuclease A]] | [[Image:1RTAnew.png|thumb|left|200px|Thymidylic acid tetramer complexed with ribonuclease A]] | ||
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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 RNase A. DNA lacks the 2’OH essential to RNA cleavage, making the complex more conducive to crystallography. <scene name=' | To determine the structural characteristics of RNA substrate binding to RNase A, X-ray crystallography was used to image inhibitory DNA tetramers bound to RNase A. DNA lacks the 2’OH essential to RNA cleavage, making the complex more conducive to crystallography. <scene name='44/449690/Cv/8'>The complex</scene> between RNase A and <scene name='44/449690/Cv/9'>thymidylic acid tetramer (d(pT)4)</scene> ([[1rta]]) provides information about 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. Examples of these interactions include hydrogen bonding between <scene name='44/449690/Cv/10'>phosphate of T1 and Arg39</scene> as well as hydrogen bonding between the O5’ oxygen of the ribose of <scene name='44/449690/Cv/12'>T3 and Lys41</scene>. <ref>PMID:1429575</ref> | ||
[[Image:1RCNnew.png|thumb|left|200px|ApTpApApG complexed with ribonuclease A]] | [[Image:1RCNnew.png|thumb|left|200px|ApTpApApG complexed with ribonuclease A]] | ||
