1TEN

STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN

Summary for 1TEN

• Entry DOI: 10.2210/pdb1ten/pdb
• Descriptor: TENASCIN (2 entities in total)
• Functional Keywords: cell adhesion protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P24821
• Total number of polymer chains: 1
• Total formula weight: 10061.06

Authors

Leahy, D.J.,Hendrickson, W.A.,Aukhil, I.,Erickson, H.P. (deposition date: 1992-08-28, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Leahy, D.J.,Hendrickson, W.A.,Aukhil, I.,Erickson, H.P.
Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.
Science, 258:987-991, 1992

PubMed 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.

PubMed: 1279805

Experimental method

X-RAY DIFFRACTION (1.8 Å)