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Search results 101 to 106 out of 106 for Dpp8

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0.017s
Type Details Score
Publication
First Author: Ross B
Year: 2018
Journal: Proc Natl Acad Sci U S A
Title: Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer.
Volume: 115
Issue: 7
Pages: E1437-E1445
Protein Domain
Type: Domain
Description: Dipeptidyl peptidase (DPP) family members 8 and 9 are similar to DPP4, consisting of one N-terminal β-propeller and a C-terminal alpha/beta hydrolase domain, which form a functional homodimer. This entry represents the N-terminal β-propeller of DPP8 and 9 which consists of eight blades and enlaces a central round pore. It provides the key arginine residue fundamental for substrate fixation which is located in the R-segment, at the interconnecting loop between blades 1 and 2. Ligand binding to DPP8/9 induces a rearrangement at the active site through a disorder-order transition in a loop segment which includes the key arginine residue and partially folds in an α-helix (R-helix) []. DPP8 and DPP9 play a role in the immune system and in preadipocyte differentiation. DPP9 is also essential for neonatal survival and plays a role in antigen maturation, cell migration, and cell adhesion.
Protein
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
Publication
First Author: Zhang H
Year: 2015
Journal: FEBS J
Title: Identification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis.
Volume: 282
Issue: 19
Pages: 3737-57
Protein
Organism: Mus musculus/domesticus
Length: 892  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 862  
Fragment?: false