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Electron microscopy and structural model of human fibronectin receptor.
M V Nermut1, N M Green, P Eason
1National Institute for Medical Research, The Ridgeway, London, UK.
The EMBO Journal
|December 20, 1988
Summary
The human fibronectin receptor, a protein complex, has a distinct structure with a globular head and two tails. Electron microscopy and computational analysis revealed details of its molecular architecture and tail composition.
Area of Science:
- Cell Biology
- Structural Biology
- Biochemistry
Background:
- The fibronectin receptor is a crucial cell surface protein involved in cell adhesion and signaling.
- Understanding its structure is key to elucidating its function in biological processes.
Purpose of the Study:
- To determine the molecular structure of the human fibronectin receptor.
- To investigate the structural characteristics of the receptor's subunits and their arrangement.
Main Methods:
- Electron microscopy was employed to visualize the purified fibronectin receptor.
- Preparative procedures were used to isolate and study the receptor complex.
- Computer-assisted structure prediction based on amino acid sequences was performed.
Main Results:
- The fibronectin receptor comprises a globular head (80x120 Å) and two tails (20 Å thick, 180-200 Å long), with the entire complex measuring approximately 280 Å.
- Receptor aggregation into doublets, triplets, or rosettes was observed at low detergent concentrations, linked via the transmembrane tails.
- Structural prediction indicated distinct secondary structures for the alpha-tail (beta-strand rich) and beta-tail (five cysteine-rich repeats, similar to laminin's EGF-like repeats).
Conclusions:
- The study provides a detailed structural model of the human fibronectin receptor, integrating electron microscopy and computational data.
- The findings highlight the structural heterogeneity of the receptor tails and their potential roles in molecular interactions and membrane anchoring.