RGD Reference Report - The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the collagen-binding site. - Rat Genome Database

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The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the collagen-binding site.

Authors: Loster, K  Zeilinger, K  Schuppan, D  Reutter, W 
Citation: Loster K, etal., Biochem Biophys Res Commun. 1995 Dec 5;217(1):341-8.
RGD ID: 1626468
Pubmed: PMID:8526932   (View Abstract at PubMed)
DOI: DOI:10.1006/bbrc.1995.2782   (Journal Full-text)

A remarkable property of the integral glycoprotein dipeptidyl peptidase IV (DPP IV, CD 26) is its affinity to proteins of the extracellular matrix (ECM). By in vitro binding assays we have shown that DPP IV binds to collagens; preferentially to the collagens I and III, which are both characterized by the formation of large triplehelical domains. No binding of DPP IV to laminin or fibronectin could be observed. Within collagen I, the alpha 1(I) chain was found to be the most prominent binding ligand of DPP IV. A monoclonal anti DPP IV antibody (13.4) specifically inhibited the interaction of DPP IV with collagen I. Peptide mapping and N-terminal sequencing revealed that the corresponding epitope of mAb 13.4 is located in the cysteine-rich domain of DPP IV. We therefore conclude that the putative collagen binding site of DPP IV is different from the region of the catalytic site containing the exopeptidase activity, which is located at the C-terminal portion of the molecule.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
collagen binding  IDA 1626468 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Dpp4  (dipeptidylpeptidase 4)


Additional Information