1ten
From Proteopedia
(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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| - | [[Image:1ten.gif|left|200px]]<br /> | + | [[Image:1ten.gif|left|200px]]<br /><applet load="1ten" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ten" size=" | + | |
caption="1ten, resolution 1.8Å" /> | caption="1ten, resolution 1.8Å" /> | ||
'''STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br /> | '''STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fibronectin type III domains are found in many different proteins | + | 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== | ==About this Structure== | ||
| - | 1TEN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1TEN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aukhil, I.]] | [[Category: Aukhil, I.]] | ||
| - | [[Category: Erickson, H | + | [[Category: Erickson, H P.]] |
| - | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
| - | [[Category: Leahy, D | + | [[Category: Leahy, D J.]] |
[[Category: cell adhesion protein]] | [[Category: cell adhesion protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:42 2008'' |
Revision as of 13:12, 21 February 2008
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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 Thu Feb 21 15:12:42 2008
