Sandbox Reserved 200: Difference between revisions

Both dimers conserve the structure of the two monomers except for the conformation at the hinge loops.  The  

<scene name='Sandbox_Reserved_200/Minor_dimer/3'>hinge loop</scene> is the location where the two monomers connect acting like the hinge of a door.<ref name="liul"/>  The most important component of the hinge loops is Ala19.  <scene name='Sandbox_Reserved_200/Minor_dimer_hinge/1'>Ala19</scene> gives these hinges their flexibility.  This flexibility allows the dimers to adopt different orientations.<ref name="liu98"/>

Not only is the structure of the monomers conserved in the dimers, but the active is also conserved. <ref name="liu98"/>  The active site of both dimers contains His12, Lys41, and His119 residues.  The active sites are a composite of the monomer subunits containing His12 from one monomer and His119 form the other monomer.<ref name="liul"/>  During domain swapping, the active site is not disturbed, so the dimers are able to retain their enzymatic activity.  In fact, the enzymatic activity of RNase oligomers is higher than that of the monomers.<ref name="liu01"/>

==Medical Relevance==

[http://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer’s disease] is a terminal disease that slowly degenerates the brain.  One of the possible causes of Alzheimer’s is [http://en.wikipedia.org/wiki/Amyloid amyloid] deposits throughout the brain.  Though RNasa A oligomers are not the amyloid deposits that cause Alzheimer’s the folding of these oligomers gives clues towards the formation of amyloid deposits responsible for Alzheimer’s.