Sandbox Reserved 194: Difference between revisions
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[[Image:1RTAnew.png|thumb|left|275px|Thymidylic acid tetramer complexed with ribonuclease A]] | [[Image:1RTAnew.png|thumb|left|275px|Thymidylic acid tetramer complexed with ribonuclease A]] | ||
== Substrate Binding == | |||
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'> | ||
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for adenosine bases at these two positions. RNase A establishes <scene name='Sandbox_Reserved_194/1rcn_his/9'>pi stacking between His119 and A3 </scene>in addition to hydrogen bonding between <scene name='Sandbox_Reserved_194/1rcn_hydrogen_bonding/9'>Asn71-A3, Gln69-A3 and Gln69-A4</scene>. ‘<ref>PMID:8063789</ref>’ | for adenosine bases at these two positions. RNase A establishes <scene name='Sandbox_Reserved_194/1rcn_his/9'>pi stacking between His119 and A3 </scene>in addition to hydrogen bonding between <scene name='Sandbox_Reserved_194/1rcn_hydrogen_bonding/9'>Asn71-A3, Gln69-A3 and Gln69-A4</scene>. ‘<ref>PMID:8063789</ref>’ | ||
== Conclusion == | |||
== References == | == References == | ||
<references/> | <references/> | ||
