6HG7
Crystal structure of a collagen II fragment containing the binding site of PEDF and COMP, (POG)4-LKG HRG FTG LQG-POG(4)
Summary for 6HG7
| Entry DOI | 10.2210/pdb6hg7/pdb |
| Descriptor | Collagen alpha-1(II) chain, SULFATE ION (3 entities in total) |
| Functional Keywords | collagen helix, collagen-like peptide, collagen ii, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 3 |
| Total formula weight | 10403.34 |
| Authors | Gebauer, J.M.,Koehler, A.,Dietmar, H.,Gompert, M.,Neundorf, I.,Zaucke, F.,Koch, M.,Baumann, U. (deposition date: 2018-08-22, release date: 2018-12-05, Last modification date: 2024-01-17) |
| Primary citation | Gebauer, J.M.,Kohler, A.,Dietmar, H.,Gompert, M.,Neundorf, I.,Zaucke, F.,Koch, M.,Baumann, U. COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens. Sci Rep, 8:17187-17187, 2018 Cited by PubMed Abstract: COMP (cartilage oligomeric matrix protein) is a member of the thrombospondin family and forms homopentamers as well as mixed heterooligomers with its closely related family member TSP-4. COMP is long known to bind to collagens and to influence collagen fibril formation. Recent work indicates that already intracellular interaction with collagen is important for collagen secretion. However, the exact binding site of COMP on the collagen triple helix has not been described up to now. In this study we have identified a GXKGHR motif on the collagen II helix to bind to COMP, using a recombinantly expressed collagen II peptide library. This binding sequence is conserved throughout evolution and we demonstrate that TSP-4 binds to the same sequence. The identified binding motif overlaps with the recognition sites of many other collagen-binding partners (e.g. PEDF, Heparin) and also spans the lysine residues, which form collagen cross-links. COMP might thereby protect collagen helices from premature modification and cross-linking. Interestingly, this motif is only found in classical fibrillar collagens, although COMP is known to also bind other types. This might indicate that COMP has a unique interface for fibrillar collagens, thus making it an interesting target for the development of antifibrotic drugs. PubMed: 30464261DOI: 10.1038/s41598-018-35447-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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