Sandbox Reserved 194: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 6: | Line 6: | ||
== Introduction == | == Introduction == | ||
<Structure load='1RTA' size='450' frame='true' align='right' caption=' | <Structure load='1RTA' size='450' frame='true' align='right' caption='Ribonuclease A complexed with thymidylic acid tetramer and ApTpApApG showing pi stacking and hydrogen bonding ' scene='Sandbox_Reserved_194/1rta_structure/2'/> | ||
RNase A is an endonuclease that cleaves and breaks down RNA using acid base catalysis (link to sandbox 193). RNase A has been a model protein for studies on the stability, folding and chemistry of proteins. ‘<ref>PMID:11848924</ref>’ It is also essential in protein regulation within the body due to its function of RNA degradation. | RNase A is an endonuclease that cleaves and breaks down RNA using acid base catalysis (link to sandbox 193). RNase A has been a model protein for studies on the stability, folding and chemistry of proteins. ‘<ref>PMID:11848924</ref>’ It is also essential in protein regulation within the body due to its function of RNA degradation. | ||
| Line 14: | Line 14: | ||
== Substrate Binding == | == 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 RNase A. DNA lacks the 2’OH essential to RNA cleavage, making the complex more conducive to crystallography. The complex between RNase A and thymidylic acid tetramer (d(pT)4) 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='Sandbox_Reserved_194/1rta_structure_arg/4'> phosphate of thymine 1 and Arg39</scene> as well as hydrogen bonding between the O5’ oxygen of the ribose of thymine 3 and Lys41. ‘<ref>PMID:1429575</ref>’ | 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. The complex between RNase A and thymidylic acid tetramer (d(pT)4) 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='Sandbox_Reserved_194/1rta_structure_arg/4'> phosphate of thymine 1 and Arg39</scene> as well as hydrogen bonding between the O5’ oxygen of the ribose of <scene name='Sandbox_Reserved_194/1rta_lys41/1'>thymine 3 and Lys41</scene>. ‘<ref>PMID:1429575</ref>’ | ||
[[Image:1RCNnew.png|thumb|left|275px|ApTpApApG complexed with ribonuclease A]] | [[Image:1RCNnew.png|thumb|left|275px|ApTpApApG complexed with ribonuclease A]] | ||
