5YQ5

Crystal structure of human osteomodulin

5YQ5 の概要

• エントリーDOI: 10.2210/pdb5yq5/pdb
• 分子名称: Osteomodulin, 2-acetamido-2-deoxy-beta-D-glucopyranose, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: collagen; fibril formation; regulation, protein fibril
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 203723.02

構造登録者

Caaveiro, J.M.M.,Tashima, T.,Tsumoto, K. (登録日: 2017-11-05, 公開日: 2018-04-25, 最終更新日: 2024-10-23)

主引用文献

Tashima, T.,Nagatoishi, S.,Caaveiro, J.M.M.,Nakakido, M.,Sagara, H.,Kusano-Arai, O.,Iwanari, H.,Mimuro, H.,Hamakubo, T.,Ohnuma, S.I.,Tsumoto, K.
Molecular basis for governing the morphology of type-I collagen fibrils by Osteomodulin.
Commun Biol, 1:33-33, 2018

PubMed Abstract: 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.

PubMed: 30271919
DOI: 10.1038/s42003-018-0038-2

実験手法

X-RAY DIFFRACTION (2.17 Å)