In silico characterization of the interaction between LSKL peptide, a LAP-TGF-beta derived peptide, and ADAMTS1
详细信息 查看全文
- 作者：Marie-Amandine Laurenta ; Dominique Bonnierb ; Nathalie Thé ; retb ; Pierre Tuffé ; rya ; Gautier Moroya ; gautier.moroy@univ-paris-diderot.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：ADAM ; a disintegrin and metalloproteinase ; ADAMTS ; ADAM with thrombospondin domains motifs ; ECM ; extracellular matrix ; LAP ; latency-associated protein ; LGAL ; amarckian genetic algorithm ; Kd ; dissociation constant ; MD ; molecular dynamics ; RMSD ; root mean square deviation ; SLC ; small latent complex ; TGF-β ; transforming growth factor ; TSP1 ; thrombospondin type-1
- 刊名：Computational Biology and Chemistry
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：61
- 期：Complete
- 页码：155-161
- 全文大小：1689 K
文摘
- •
We have experimentally shown that TSP-1 domain of ADAMTS1 is able to bind TGF-β.
- •
Docking experiments confirm that KTFR sequence interacts with LSKL peptide.
- •
MD simulations reach a stable binding mode between TSP-1 domain and LSKL peptide.