1TTG
THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS
Summary for 1TTG
| Entry DOI | 10.2210/pdb1ttg/pdb |
| Descriptor | FIBRONECTIN (1 entity in total) |
| Functional Keywords | glycoprotein |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix: P02751 |
| Total number of polymer chains | 1 |
| Total formula weight | 9947.06 |
| Authors | Main, A.L.,Harvey, T.S.,Baron, M.,Campbell, I.D. (deposition date: 1993-07-14, release date: 1994-01-31, Last modification date: 2024-05-01) |
| Primary citation | Main, A.L.,Harvey, T.S.,Baron, M.,Boyd, J.,Campbell, I.D. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell(Cambridge,Mass.), 71:671-678, 1992 Cited by PubMed Abstract: The solution structure of the tenth type III module of fibronectin has been determined using nuclear magnetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven beta strands forming two antiparallel beta sheets, which pack against each other. Both beta sheets contribute conserved hydrophobic residues to a compact core. The topology is more similar to that of domain 2 of CD4, PapD, and the extracellular domain of the human growth hormone receptor than to that of immunoglobulin C domains. The module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion. This tripeptide is solvent exposed and lies on a conformationally mobile loop between strands F and G, consistent with its cell adhesion function. PubMed: 1423622DOI: 10.1016/0092-8674(92)90600-H PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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