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

Publication ,  Journal Article
Leahy, DJ; Hendrickson, WA; Aukhil, I; Erickson, HP
Published in: Science
November 6, 1992

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.

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Published In

Science

DOI

ISSN

0036-8075

Publication Date

November 6, 1992

Volume

258

Issue

5084

Start / End Page

987 / 991

Location

United States

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

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Leahy, D. J., Hendrickson, W. A., Aukhil, I., & Erickson, H. P. (1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science, 258(5084), 987–991. https://doi.org/10.1126/science.1279805
Leahy, D. J., W. A. Hendrickson, I. Aukhil, and H. P. Erickson. “Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.Science 258, no. 5084 (November 6, 1992): 987–91. https://doi.org/10.1126/science.1279805.
Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. 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.
Leahy, D. J., et al. “Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.Science, vol. 258, no. 5084, Nov. 1992, pp. 987–91. Pubmed, doi:10.1126/science.1279805.
Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science. 1992 Nov 6;258(5084):987–991.
Journal cover image

Published In

Science

DOI

ISSN

0036-8075

Publication Date

November 6, 1992

Volume

258

Issue

5084

Start / End Page

987 / 991

Location

United States

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