TY - JOUR
T1 - Molecular basis for governing the morphology of type-I collagen fibrils by Osteomodulin
AU - Tashima, Takumi
AU - Nagatoishi, Satoru
AU - Caaveiro, Jose M.M.
AU - Nakakido, Makoto
AU - Sagara, Hiroshi
AU - Kusano-Arai, Osamu
AU - Iwanari, Hiroko
AU - Mimuro, Hitomi
AU - Hamakubo, Takao
AU - Ohnuma, Shin ichi
AU - Tsumoto, Kouhei
N1 - Funding Information:
This work was supported by the Funding program for world-leading Innovative R&D on Science and Technology (FIRST) from JSPS, the Platform for Drug Discovery, Informatics, and Structural Life Science (MEXT), JSPS Grants-in-Aid for Scientific Research 16H02420 (K.T.), 15K17882 (S.N.), 15K06962 (J.M.M.C.), and a Grant-in-Aid for JSPS fellows (T.T.). Access to beamline AR-NE3A was granted by the Photon Factory Advisory Committee (Proposal 2013G178).
Publisher Copyright:
© 2018, The Author(s).
PY - 2018/12/1
Y1 - 2018/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85070938496&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85070938496&partnerID=8YFLogxK
U2 - 10.1038/s42003-018-0038-2
DO - 10.1038/s42003-018-0038-2
M3 - Article
C2 - 30271919
AN - SCOPUS:85070938496
SN - 2399-3642
VL - 1
JO - Communications Biology
JF - Communications Biology
IS - 1
M1 - 33
ER -