Molecular basis for governing the morphology of type-I collagen fibrils by Osteomodulin

Takumi Tashima, Satoru Nagatoishi, Jose M.M. Caaveiro, Makoto Nakakido, Hiroshi Sagara, Osamu Kusano-Arai, Hiroko Iwanari, Hitomi Mimuro, Takao Hamakubo, Shin ichi Ohnuma, Kouhei Tsumoto

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


Small leucine-rich repeat proteoglycan (SLRP) proteins have an important role in the organization of the extracellular matrix, especially in the formation of collagen fibrils. However, the mechanism governing the shape of collagen fibrils is poorly understood. Here, we report that the protein Osteomodulin (OMD) of the SLRP family is a monomeric protein in solution that interacts with type-I collagen. This interaction is dominated by weak electrostatic forces employing negatively charged residues of OMD, in particular Glu284 and Glu303, and controlled by entropic factors. The protein OMD establishes a fast-binding equilibrium with collagen, where OMD may engage not only with individual collagen molecules, but also with the growing fibrils. This weak electrostatic interaction is carefully balanced so it modulates the shape of the fibrils without compromising their viability.

Original languageEnglish
Article number33
JournalCommunications Biology
Issue number1
Publication statusPublished - Dec 1 2018

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • Medicine (miscellaneous)


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