5YQ5
Crystal structure of human osteomodulin
Summary for 5YQ5
| Entry DOI | 10.2210/pdb5yq5/pdb |
| Descriptor | Osteomodulin, 2-acetamido-2-deoxy-beta-D-glucopyranose, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | collagen; fibril formation; regulation, protein fibril |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 203723.02 |
| Authors | Caaveiro, J.M.M.,Tashima, T.,Tsumoto, K. (deposition date: 2017-11-05, release date: 2018-04-25, Last modification date: 2024-10-23) |
| Primary citation | 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 Cited by 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: 30271919DOI: 10.1038/s42003-018-0038-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.17 Å) |
Structure validation
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