Prediction of dipeptidyl peptidase (DP) 8 structure by homology modelling.
Pitman
Melissa R
MR
Flinders University, School of Biological Sciences, Flinders University, Adelaide, SA, Australia.
Menz
R Ian
RI
Abbott
Catherine A
CA
D001665:Binding Sites; D004150:Dipeptidases / Q000737:chemistry* / Q000235:genetics; D018819:Dipeptidyl Peptidase 4 / Q000737:chemistry / Q000235:genetics; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics; D010447:Peptide Hydrolases / Q000737:chemistry / Q000235:genetics; D015221:Potassium Channels / Q000737:chemistry / Q000235:genetics; D000085822:Prolyl Oligopeptidases; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics
D009419:Nerve Tissue Proteins; D015221:Potassium Channels; C503535:DPP6 protein, human; D010447:Peptide Hydrolases; D004150:Dipeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C487997:DPP8 protein, human; D018819:Dipeptidyl Peptidase 4; C038220:acylaminoacyl-peptidase; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases