5MX0
Crystal structure of human fibromodulin
Summary for 5MX0
| Entry DOI | 10.2210/pdb5mx0/pdb |
| Descriptor | Fibromodulin, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | leucine-rich repeat, extracellular matrix, collagen binding, structural protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted, extracellular space, extracellular matrix: Q06828 |
| Total number of polymer chains | 2 |
| Total formula weight | 87669.12 |
| Authors | Paracuellos, P.,Hohenester, E. (deposition date: 2017-01-20, release date: 2017-03-01, Last modification date: 2024-11-13) |
| Primary citation | Paracuellos, P.,Kalamajski, S.,Bonna, A.,Bihan, D.,Farndale, R.W.,Hohenester, E. Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin. Matrix Biol., 63:106-116, 2017 Cited by PubMed Abstract: The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2Å resolution of human fibromodulin and chondroadherin, two collagen-binding SLRPs. Their overall fold is similar to that of the prototypical SLRP, decorin, but unlike decorin neither fibromodulin nor chondroadherin forms a stable dimer. A previously identified binding site for integrin α2β1 maps to an α-helix in the C-terminal cap region of chondroadherin. Interrogation of the Collagen Toolkits revealed a unique binding site for chondroadherin in collagen II, and no binding to collagen III. A triple-helical peptide containing the sequence GAOGPSGFQGLOGPOGPO (O is hydroxyproline) forms a stable complex with chondroadherin in solution. In fibrillar collagen I and II, this sequence is aligned with the collagen cross-linking site KGHR, suggesting a role for chondroadherin in cross-linking. PubMed: 28215822DOI: 10.1016/j.matbio.2017.02.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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