Sandbox Reserved 918: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 6: Line 6:
=Dipeptidyl Peptidase IV=
=Dipeptidyl Peptidase IV=


[[Image:DPP4_image.png|300px|right|thumb|<font size="3.5"><div style="text-align: center;"> [http://en.wikipedia.org/wiki/Ribbon_diagram Ribbon diagram] of DPP IV from PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=1PFQ 1PFQ] </div></font>]]
[[Image:1x70_dimer.png|300px|right|thumb|<font size="3.5"><div style="text-align: center;"> [[Cartoon backbone representation | Cartoon representation]] of DPP-IV designed in [http://www.pymol.org/ PyMol] from [http://en.wikipedia.org/wiki/Protein_Data_Bank PDB] [http://www.rcsb.org/pdb/explore/explore.do?structureId=1X70 1X70] </div></font>]]


===Introduction===
===Introduction===
'''Dipeptidyl Peptidase IV''' (commonly abbreviated as '''DPP IV''') is a regulatory [http://en.wikipedia.org/wiki/Protease protease] and binding [http://en.wikipedia.org/wiki/Protein protein] that carries out numerous functions in humans making it a prime candidate for medicinal and pharmaceutical research. DPP IV, discovered by V.K. Hopsu-Havu and G.G. Glenner in homogenized rat liver tissue, was originally believed to serve a specific role in breaking [http://en.wikipedia.org/wiki/2-Naphthylamine 2-Naphthylamine] off of [http://brenda-enzymes.org/php/ligand_flatfile.php4?brenda_ligand_id=228740 Gly-Pro-2-napthylamide], hence its original name glycylproline napthylamidase. However, further research into the specificity of DPP IV eventually showed that it serves a more generic function as a [http://en.wikipedia.org/wiki/Hydrolase hydrolase] (a serine [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), breaking  N-terminal Xaa-Pro bonds. These penultimate [http://en.wikipedia.org/wiki/Proline prolines] of the [http://en.wikipedia.org/wiki/N-terminus N-terminus] are known for their ability to resist attacks from most proteases and also induce a [http://en.wikipedia.org/wiki/Conformational_change conformational change] of their respective proteins. Therefore, DPP IV and its ability to catalyze said prolines gives it a unique specificity and target for pharmaceutical companies to take advantage of. <ref> Mentlein, R. (1999). Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides. Regulatory Peptides, 85(1), 9–24. http://www.sciencedirect.com/science/article/pii/S0167011599000890 </ref>
'''Dipeptidyl Peptidase IV''' (commonly abbreviated as '''DPP IV''') is a regulatory [http://en.wikipedia.org/wiki/Protease protease] and binding [http://en.wikipedia.org/wiki/Glycoprotein glycoprotein] that carries out numerous functions in humans making it a prime candidate for medicinal and pharmaceutical research. DPP IV, discovered by V.K. Hopsu-Havu and G.G. Glenner in homogenized rat liver tissue, was originally believed to serve a specific role in breaking [http://en.wikipedia.org/wiki/2-Naphthylamine 2-Naphthylamine] off of [http://brenda-enzymes.org/php/ligand_flatfile.php4?brenda_ligand_id=228740 Gly-Pro-2-napthylamide], hence its original name glycylproline napthylamidase. However, further research into the specificity of DPP IV eventually showed that it serves a more generic function as a [http://en.wikipedia.org/wiki/Hydrolase hydrolase] (a serine [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), breaking  N-terminal Xaa-Pro bonds. These penultimate [http://en.wikipedia.org/wiki/Proline prolines] of the [http://en.wikipedia.org/wiki/N-terminus N-terminus] are known for their ability to resist attacks from most proteases and also induce a [http://en.wikipedia.org/wiki/Conformational_change conformational change] of their respective proteins. Therefore, DPP IV and its ability to catalyze said prolines gives it a unique specificity and target for pharmaceutical companies to take advantage of. <ref> Mentlein, R. (1999). Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides. Regulatory Peptides, 85(1), 9–24. http://www.sciencedirect.com/science/article/pii/S0167011599000890 </ref>


===Structure===
===Structure===
===Medical Relevancy===
===Medical Relevancy===
===References===  
===References===  
{{reflist}}
{{reflist}}