Substrate Recognition by the Collagen-binding Domain of Clostridium histolyticum Class I Collagenase

Osamu Matsushita*, Takaki Koide, Ryoji Kobayashi, Kazuhiro Nagata, Akinobu Okabe


研究成果: Article査読

106 被引用数 (Scopus)


Clostridium histolyticum type I collagenase (ColG) has a segmental structure, S1+S2+S3a+S3b. S3a and S3b bound to insoluble collagen, but S2 did not, thus indicating that S3 forms a collagen-binding domain (CBD). Because S3a+S3b showed the most efficient binding to substrate, cooperative binding by both domains was suggested for the enzyme. Monomeric (S3b) and tandem (S3a+S3b) CBDs bound to atelocollagen, which contains only the collagenous region. However, they did not bind to telopeptides immobilized on Sepharose beads. These results suggested that the binding site(s) for the CBD is(are) present in the collagenous region. The CBD bound to immobilized collagenous peptides, (Pro-Hyp-Gly)n and (Pro-Pro-Gly)n, only when n is large enough to allow the peptides to have a triple-helical conformation. They did not bind to various peptides with similar amino acid sequences or to gelatin, which lacks a triple-helical conformation. The CBD did not bind to immobilized Glc-Gal disaccharide, which is attached to the side chains of hydroxylysine residues in the collagenous region. These observations suggested that the CBD specifically recognizes the triple-helical conformation made by three polypeptide chains in the collagenous region.

ジャーナルJournal of Biological Chemistry
出版ステータスPublished - 2001 3月 23

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学


「Substrate Recognition by the Collagen-binding Domain of Clostridium histolyticum Class I Collagenase」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。