Sandbox Reserved 194: Difference between revisions
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== '''Ribonuclease A Substrate Binding''' == | == '''Ribonuclease A Substrate Binding''' == | ||
== Headline text == | |||
<Structure load='1RTA' size='400' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_194/1rta_just_dt/1' /> | |||
[[Image:1RTA_zoom.png|thumb|left|250px|Thymidylic acid tetramer complexed with ribonuclease A]] | [[Image:1RTA_zoom.png|thumb|left|250px|Thymidylic acid tetramer complexed with ribonuclease A]] | ||
< | 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, the RNase A - <scene name='Sandbox_Reserved_194/1rta_structure/1'>thymidylic acid tetramer</scene> (d(pT)4) complex has provided information into the specificity of the binding pocket subunits, B0, B1, B2 and B3. | ||
[[Image:1RCN_zoom.png|thumb|left|250px|ApTpApApG complexed with ribonuclease A]] | [[Image:1RCN_zoom.png|thumb|left|250px|ApTpApApG complexed with ribonuclease A]] | ||
<Structure load='1RCN' size='400' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_194/1rcn_just_dtda/1' /> | <Structure load='1RCN' size='400' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_194/1rcn_just_dtda/1' /> | ||
