Sandbox Reserved 200: Difference between revisions
Lexi Gehring (talk | contribs) No edit summary |
Lexi Gehring (talk | contribs) No edit summary |
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Similar to dimer, the structure of the monomer is conserved except for the <scene name='Sandbox_Reserved_200/Minor_trimer/2'>hinge loop</scene>. The <scene name='Sandbox_Reserved_200/Minor_trimer/3'>active sites</scene> of the trimers are made up of the same amino acid residues as the monomers and dimers. | Similar to dimer, the structure of the monomer is conserved except for the <scene name='Sandbox_Reserved_200/Minor_trimer/2'>hinge loop</scene>. The <scene name='Sandbox_Reserved_200/Minor_trimer/3'>active sites</scene> of the trimers are made up of the same amino acid residues as the monomers and dimers. The trimer's active site is slightly different from that of the monomer and dimer because it has a sulfate ion trap.<ref name="liu01"/> | ||
==Medical Relevance== | ==Medical Relevance== | ||
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The 3D domain swapping has many similarities with the formation of amyloid fibers. Both are highly specific reactions coming from only one type of monomer and these reactions can form linear aggregates. <ref name="liu01"/> These aggregates of proteins are formed by hydrogen bonding at the hinge loops which form an antiparalell β-pleated sheet. <ref name="liu01"/> This most commonly happens with the major dimer. Liu suggests that all proteins are capable of forming aggregates by domain swapping as long as they are in high concentration and partially destabilized. <ref name="liu01"/> As 3D domain swapping becomes more understood, it will offer insight to the amyloid formation in Alzheimer’s patients. | The 3D domain swapping has many similarities with the formation of amyloid fibers. Both are highly specific reactions coming from only one type of monomer and these reactions can form linear aggregates. <ref name="liu01"/> These aggregates of proteins are formed by hydrogen bonding at the hinge loops which form an antiparalell β-pleated sheet. <ref name="liu01"/> This most commonly happens with the major dimer. Liu suggests that all proteins are capable of forming aggregates by domain swapping as long as they are in high concentration and partially destabilized. <ref name="liu01"/> Forty different proteins who form oligomers by 3D domain swapping have already been identified.<ref name="multimers">PMID:15104538</ref > As 3D domain swapping becomes more understood, it will offer insight to the amyloid formation in Alzheimer’s patients. | ||