CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.90 | Alpha-Beta Complex | |
3.90.70 | Cathepsin B; Chain A | |
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
Superfamily | Cysteine proteinases |
Functional Family |
Enzyme Information
3.4.22.65 |
Peptidase 1 (mite).
based on mapping to UniProt P08176
Broad endopeptidase specificity.
-!- This enzyme, derived from the house dust mite, is a major component of the allergic immune response. -!- The substrate specificity of this enzyme is not altogether clear; it cleaves the low-affinity IgE receptor CD23 at 298-Glu-|-Ser-299 and 155-Ser-|-Ser-156. -!- It also cleaves the pulmonary structural proteins occludin and claudin at Leu-|-Leu, Asp-|-Leu and at Gly-|-Thr bonds, and it can also cleave the alpha subunit of the interleukin-2 (IL-2) receptor (CD25). -!- Using a positional scanning combinatorial library, it was found that the major substrate-specificity determinant is for Ala in the P2 position. -!- The enzyme shows only a slight preference for basic amino acids in the P1 and P3 positions and a preference for aliphatic amino acids such as Ile, Pro, Val, Leu and norleucine in the P4 position. -!- Belongs to peptidase family C1.
|
UniProtKB Entries (1)
P08176 |
PEPT1_DERPT
Dermatophagoides pteronyssinus
Peptidase 1
|
PDB Structure
PDB | 2AS8 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Pichia |
Primary Citation |
Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen
J.Allergy Clin.Immunol.
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