Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.
Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved by multiwavelength anomalous diffraction (MAD) phasing of the selenomethionyl protein and has been refined to 1.8 angstrom resolution. The folding topology of this domain is identical to that of the extracellular domains of the human growth hormone receptor, the second domain of CD4, and PapD. Although distinct, this topology is similar to that of immunoglobulin constant domains. An Arg-Gly-Asp (RGD) sequence that can function for cell adhesion is found in a tight turn on an exposed loop.
Duke Scholars
Altmetric Attention Stats
Dimensions Citation Stats
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- X-Ray Diffraction
- Tenascin
- Recombinant Proteins
- Receptors, Somatotropin
- Protein Structure, Secondary
- Protein Folding
- Molecular Structure
- Molecular Sequence Data
- Models, Molecular
- Magnetic Resonance Spectroscopy
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- X-Ray Diffraction
- Tenascin
- Recombinant Proteins
- Receptors, Somatotropin
- Protein Structure, Secondary
- Protein Folding
- Molecular Structure
- Molecular Sequence Data
- Models, Molecular
- Magnetic Resonance Spectroscopy