Sandbox Reserved 918: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 57: | Line 57: | ||
Lastly, the [http://en.wikipedia.org/wiki/Protein_dimer homodimerization] of DPP IV is critical to the catalytic function. Though there are domains that play key roles in the formation of this dimer, a particular histadine (<scene name='57/573132/1x70_his750/1'>His750</scene>) has been shown to inhibit the formation of the dimer if [http://en.wikipedia.org/wiki/Point_mutation point mutated] to glutamate. From this information it could be extrapolated that the histadine is forming some [http://en.wikipedia.org/wiki/Ionic_bonding ionic] interaction with the opposing chain, with the mutation from positive charge to negative charge creating a repulsive effect thus eliminating the ability to dimerize. | Lastly, the [http://en.wikipedia.org/wiki/Protein_dimer homodimerization] of DPP IV is critical to the catalytic function. Though there are domains that play key roles in the formation of this dimer, a particular histadine (<scene name='57/573132/1x70_his750/1'>His750</scene>) has been shown to inhibit the formation of the dimer if [http://en.wikipedia.org/wiki/Point_mutation point mutated] to glutamate. From this information it could be extrapolated that the histadine is forming some [http://en.wikipedia.org/wiki/Ionic_bonding ionic] interaction with the opposing chain, with the mutation from positive charge to negative charge creating a repulsive effect thus eliminating the ability to dimerize. | ||
===Propeller Domains=== | |||
</StructureSection> | </StructureSection> | ||
===Medical Relevancy=== | ===Medical Relevancy=== | ||
<scene name='57/573132/1x70_sitagliptin/1'>Sitagliptin</scene> | |||
===References=== | ===References=== | ||
{{reflist}} | {{reflist}} | ||
