2009年4月
Unidirectional binding of clostridial collagenase to triple helical substrates.
Journal of Biological Chemistry
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- 巻
- 284
- 号
- 16
- 開始ページ
- 10868
- 終了ページ
- 10876
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.m807684200
- 出版者・発行元
- Elsevier BV
Histotoxic clostridia produce collagenases responsible for extensive tissue destruction in gas gangrene. The C-terminal collagen-binding domain (CBD) of these enzymes is the minimal segment required to bind to collagen fibril. Collagen binding efficiency of CBD is more pronounced in the presence of Ca2+. We have shown that CBD can be functional to anchor growth factors in local tissue. A H-1-N-15 HSQC NMR titration study with three different tropocollagen analogues ((POG)(10))(3), ((GPOG)(7)PRG)(3), and (GPRG(POG)(7)C-carbamidomethyl)(3), mapped a saddle-like binding cleft on CBD. NMR titrations with three nitroxide spin-labeled analogues of collagenous peptide, (PROXYL-G(POG)(7)PRG)(3), (PROXYL-G(POG)(7))(3), and (GPRG(POG)(7)C-PROXYL)(3) (where PROXYL represents 2,2,5,5-tetramethyl-L-pyrrolidinyloxy), unambiguously demonstrated unidirectional binding of CBD to the tropocollagen analogues. Small angle x-rays cattering data revealed that CBD binds closer to a terminus for each of the five different tropocollagen analogues, which in conjunction with NMR titration studies, implies a binding mode where CBD binds to the C terminus of the triple helix.
- リンク情報
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- DOI
- https://doi.org/10.1074/jbc.m807684200
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/19208618
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2667773
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000265104600060&DestApp=WOS_CPL
- URL
- https://syndication.highwire.org/content/doi/10.1074/jbc.M807684200
- ID情報
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- DOI : 10.1074/jbc.m807684200
- ISSN : 0021-9258
- eISSN : 1083-351X
- PubMed ID : 19208618
- PubMed Central 記事ID : PMC2667773
- Web of Science ID : WOS:000265104600060