1ten
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(New page: 200px<br /> <applet load="1ten" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ten, resolution 1.8Å" /> '''STRUCTURE OF A FIBRO...)
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Revision as of 17:17, 12 November 2007
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STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
Overview
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.
About this Structure
1TEN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein., Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP, Science. 1992 Nov 6;258(5084):987-91. PMID:1279805
Page seeded by OCA on Mon Nov 12 19:23:48 2007
