Sandbox Reserved 194: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 9: Line 9:
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.   
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.   


Further binding pocket characterization was accomplished using the oglionucleotide d(ApTpApApG).  While binding of other nucleobases to the B2 and B3 sites is possible, the imaging of this complex elucidated the preference for adenosine bases.  RNase A establishes <scene name='Sandbox_Reserved_194/1rcn_his/4'>pi stacking between His119 and A3</scene> in addition to hydrogen bonding between Asn71-A3, Gln69-A3 and Gln69-A4.
Further binding pocket characterization was accomplished using the oglionucleotide <scene name='Sandbox_Reserved_194/1rcn_just_dtda/1'>d(ApTpApApG)</scene>.  While binding of other nucleobases to the B2 and B3 sites is possible, the imaging of this <scene name='Sandbox_Reserved_194/1rcn_structure/2'>complex</scene> elucidated the preference for adenosine bases.  RNase A establishes <scene name='Sandbox_Reserved_194/1rcn_his/4'>pi stacking between His119 and A3</scene> in addition to hydrogen bonding between Asn71-A3, Gln69-A3 and Gln69-A4.
[[Image:1RCN_zoom.png|thumb|left|250px|ApTpApApG complexed with ribonuclease A]]
[[Image:1RCN_zoom.png|thumb|left|250px|ApTpApApG complexed with ribonuclease A]]