Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein

Science. 1992 Nov 6;258(5084):987-91. doi: 10.1126/science.1279805.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Adhesion Molecules, Neuronal / chemistry*
  • Chickens
  • Crystallization
  • Escherichia coli / genetics
  • Extracellular Matrix Proteins / chemistry*
  • Fibronectins / chemistry*
  • Humans
  • Immunoglobulin Constant Regions / chemistry
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Protein Folding
  • Protein Structure, Secondary
  • Receptors, Somatotropin / chemistry
  • Recombinant Proteins / chemistry
  • Tenascin
  • X-Ray Diffraction*


  • Cell Adhesion Molecules, Neuronal
  • Extracellular Matrix Proteins
  • Fibronectins
  • Immunoglobulin Constant Regions
  • Receptors, Somatotropin
  • Recombinant Proteins
  • Tenascin