1UZJ
Integrin binding cbEGF22-TB4-cbEGF33 fragment of human fibrillin-1, holo form.
Summary for 1UZJ
| Entry DOI | 10.2210/pdb1uzj/pdb |
| Related | 1APJ 1EMN 1EMO 1LMJ 1UZK 1UZP 1UZQ |
| Descriptor | FIBRILLIN-1, CALCIUM ION (3 entities in total) |
| Functional Keywords | matrix protein, extra-cellular matrix, fibrillin-1, cbegf domain, tb domain matrix protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Secreted, extracellular space, extracellular matrix: P35555 |
| Total number of polymer chains | 3 |
| Total formula weight | 52237.78 |
| Authors | Lee, S.S.J.,Knott, V.,Harlos, K.,Handford, P.A.,Stuart, D.I. (deposition date: 2004-03-12, release date: 2004-04-08, Last modification date: 2024-10-16) |
| Primary citation | Lee, S.S.J.,Knott, V.,Jovanovi, J.,Harlos, K.,Grimes, J.,Choulier, L.,Mardon, H.,Stuart, D.I.,Handford, P.A. Structure of the Integrin Binding Fragment from Fibrillin-1 Gives New Insights Into Microfibril Organization Structure, 12:717-, 2004 Cited by PubMed Abstract: Human fibrillin-1, the major structural protein of extracellular matrix (ECM) 10-12 nm microfibrils, is dominated by 43 calcium binding epidermal growth factor-like (cbEGF) and 7 transforming growth factor beta binding protein-like (TB) domains. Crystal structures reveal the integrin binding cbEGF22-TB4-cbEGF23 fragment of human fibrillin-1 to be a Ca(2+)-rigidified tetragonal pyramid. We suggest that other cbEGF-TB pairs within the fibrillins may adopt a similar orientation to cbEGF22-TB4. In addition, we have located a flexible RGD integrin binding loop within TB4. Modeling, cell attachment and spreading assays, immunocytochemistry, and surface plasmon resonance indicate that cbEGF22 bound to TB4 is a requirement for integrin activation and provide insight into the molecular basis of the fibrillin-1 interaction with alphaVbeta3. In light of our data, we propose a novel model for the assembly of the fibrillin microfibril and a mechanism to explain its extensibility. PubMed: 15062093DOI: 10.1016/J.STR.2004.02.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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