Title : The structure and function of human
dipeptidyl peptidase IV , possessing a unique eight-bladed beta-propeller fold
Abstract :
- Dipeptidyl peptidase IV ( DPPIV ) is a serine protease , a member of the prolyl oligopeptidase (POP) family, and has been implicated in several diseases
- Therefore, the development of DPPIV selective inhibitors, which are able to control the biological function of DPPIV , is important
- We determined the crystal structure of human DPPIV at 2.6A resolution
- The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region
- Also, the large "cave" structure, which is thought to control the access of the substrate, is found on the side of the beta-propeller fold
- Comparison of the overall amino acid sequence between human DPPIV and POP shows low homology (12.9%)
- In this paper, we report the structure of human DPPIV , especially focusing on a unique eight-bladed beta-propeller domain
- We also discuss the way for the access of the substrate to this domain
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
- 4. -, region
- 4. protease, domain
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):