Sandbox Reserved 918

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===Structure===
===Structure===
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<Structure load='1X70' size='350' frame='true' align='right' caption='Biological Dimer of DPP IV' scene='Insert optional scene name here' />
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</StructureSection>
===Medical Relevancy===
===Medical Relevancy===
===References===
===References===
{{reflist}}
{{reflist}}

Revision as of 12:15, 25 March 2014

This Sandbox is Reserved from Jan 06, 2014, through Aug 22, 2014 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 911 through Sandbox Reserved 922.
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Contents

Dipeptidyl Peptidase IV

Image:1x70 dimer.png
Cartoon representation of DPP-IV designed in PyMol from PDB 1X70

Introduction

Dipeptidyl Peptidase IV (commonly abbreviated as DPP IV) is a regulatory protease and binding 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 2-Naphthylamine off of 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 hydrolase (a serine exopeptidase), breaking N-terminal Xaa-Pro bonds. These penultimate prolines of the N-terminus are known for their ability to resist attacks from most proteases and also induce a 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. [1]

Structure

Biological Dimer of DPP IV

Drag the structure with the mouse to rotate

</StructureSection>

Medical Relevancy

References

  1. ↑ 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
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