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

Author information

Affiliations

  • 1. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
      Authors
    • Leahy DJ 1
    (1 author)

Science, 01 Nov 1992, 258(5084):987-991
https://doi.org/10.1126/science.1279805 PMID: 1279805 

Abstract 

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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Read article at publisher's site: https://doi.org/10.1126/science.1279805

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Funding 

Funders who supported this work.

NCI NIH HHS (1)

NIDCR NIH HHS (1)

NIGMS NIH HHS (1)