1QO6
Solution structure of a pair of modules from the gelatin-binding domain of fibronectin
Summary for 1QO6
| Entry DOI | 10.2210/pdb1qo6/pdb |
| Related | 1FBR 1FNA 1FNF 1FNH 1TTF 1TTG 2FN2 |
| Descriptor | FIBRONECTIN (1 entity in total) |
| Functional Keywords | cell adhesion protein, fibronectin module pair, gelatin-binding |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Secreted, extracellular space, extracellular matrix: P02751 |
| Total number of polymer chains | 1 |
| Total formula weight | 11186.24 |
| Authors | Bocquier, A.A.,Potts, J.R.,Pickford, A.R.,Campbell, I.D. (deposition date: 1999-11-04, release date: 2000-01-11, Last modification date: 2024-11-13) |
| Primary citation | Bocquier, A.A.,Potts, J.R.,Pickford, A.R.,Campbell, I.D. Solution Structure of a Pair of Modules from the Gelatin-Binding Domain of Fibronectin Structure, 7:1451-, 1999 Cited by PubMed Abstract: Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen. PubMed: 10647176DOI: 10.1016/S0969-2126(00)88336-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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