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Science 6 November 1992:
Vol. 258. no. 5084, pp. 987 - 991
DOI: 10.1126/science.1279805
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Articles

Science, Vol 258, Issue 5084, 987-991
Copyright © 1992 by American Association for the Advancement of Science

articles

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

DJ Leahy, WA Hendrickson, I Aukhil, and HP Erickson

Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.

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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