Sandbox Reserved 918: Difference between revisions
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In addition to the glutamates holding the substrate in close proximity, and the catalytic triad using acid base chemistry to cleave the peptide bond, there is a tyrosine, <scene name='57/573132/1x70_activesitetyr/5'>Tyr547</scene>, which is depicted in orange and notably only 4.08 [http://en.wikipedia.org/wiki/Angstrom angstroms] away from the substrate, [http://en.wikipedia.org/wiki/Sitagliptin Sitagliptin]. Based off of the crystal structure, this tyrosine is believed to stabilize the tetrahedral oxyanion intermediate, another important function in enzymatic processes. <ref name="Tyrosine">PMID: 15175333</ref> The active site in its entirety is considered to contain residues 39-51 and 501-766 and is known as the <scene name='57/573132/1x70_alphabetaprop/1'>α/β-hydrolase domain</scene> | In addition to the glutamates holding the substrate in close proximity, and the catalytic triad using acid base chemistry to cleave the peptide bond, there is a tyrosine, <scene name='57/573132/1x70_activesitetyr/5'>Tyr547</scene>, which is depicted in orange and notably only 4.08 [http://en.wikipedia.org/wiki/Angstrom angstroms] away from the substrate, [http://en.wikipedia.org/wiki/Sitagliptin Sitagliptin]. Based off of the crystal structure, this tyrosine is believed to stabilize the tetrahedral oxyanion intermediate, another important function in enzymatic processes. <ref name="Tyrosine">PMID: 15175333</ref> The active site in its entirety is considered to contain residues 39-51 and 501-766 and is known as the <scene name='57/573132/1x70_alphabetaprop/1'>α/β-hydrolase domain</scene> | ||
Lastly, the <scene name='57/573132/1x70_basic_dimer/1'>homodimerization</scene> (colored by monomer) of DPP IV is critical to the catalytic function. The hydrolase domain and the propeller domain are involved in the dimerization of DPP IV. Residues like<scene name='57/573132/1x70_dimerizationaa/1'>Phe713, Trp734, and Tyr735</scene> provide hydrophobic interactions that are essential for forming the dimer. (CITE chia-hui article) Though whole domains play key roles in the formation of this dimer, single residues like <scene name='57/573132/1x70_his750/2'>His750</scene> have also been shown to be key to formation of the dimer. If [http://en.wikipedia.org/wiki/Point_mutation point mutated] to glutamate, the dimer will not form. The [http://en.wikipedia.org/wiki/Ionic_bonding ionic] interactions of the histidine with the opposing chain are changed from electrostatically positive to a repulsive effect thus eliminating the ability to dimerize. <ref name="Gorrell"/> | Lastly, the <scene name='57/573132/1x70_basic_dimer/1'>homodimerization</scene> (colored by monomer) of DPP IV is critical to the catalytic function. The hydrolase domain and the propeller domain are involved in the dimerization of DPP IV. Residues like <scene name='57/573132/1x70_dimerizationaa/1'>Phe713, Trp734, and Tyr735</scene> provide hydrophobic interactions that are essential for forming the dimer. (CITE chia-hui article) Though whole domains play key roles in the formation of this dimer, single residues like <scene name='57/573132/1x70_his750/2'>His750</scene> have also been shown to be key to formation of the dimer. If [http://en.wikipedia.org/wiki/Point_mutation point mutated] to glutamate, the dimer will not form. The [http://en.wikipedia.org/wiki/Ionic_bonding ionic] interactions of the histidine with the opposing chain are changed from electrostatically positive to a repulsive effect thus eliminating the ability to dimerize. <ref name="Gorrell"/> | ||
===Propeller Domain=== | ===Propeller Domain=== | ||