RNaseS RNaseB: Difference between revisions

[[Image:surface view of rnase s.png|200px|left|thumb|  The surface interaction between the S peptide and S protein fragments; S peptide is blue, S protein is yellow.]]

RNase A and RNase S have very similar structures except for a few key areas, one being the cleavage site (residues 16-23)<ref name="Raines"> PMID:11848924</ref>.  Decreased order in these amino acids is seen in RNase S.  The <scene name='Sandbox_Reserved_195/Clevage_site/4' target='0'>cleavage site</scene> on RNase A is located between residues Ala 20 and Ser 21.  Upon cleavage, the fragments S peptide and S protein are created, giving RNase S its unique structure.  <scene name='Sandbox_Reserved_195/S_peptide/8' target='0'>S Peptide</scene> consists of residues 1-20, and is largely responsible for proper folding.  <scene name='Sandbox_Reserved_195/S_protein/2'>S protein</scene> is comprised of residues 21-124.  Additionally, RNase A and RNase S have many conserved structural components, as they are essentially the same protein.  Glutamine 60 is highly conserved structurally between  <scene name='Sandbox_Reserved_195/Gln_60/3' target='0'>RNase S</scene> and <scene name='Sandbox_Reserved_195/Glutamine_60_rnase_a/5' target='0'>RNase A</scene>, as well as in many different species, demonstrating its importance.  Glu 60 is also interesting, because it is the only residue in an unfavorable position (Φ= -100, ψ= -130) as defined in the Ramachandran plot <ref name="Kim">PMID:1463719</ref>.