1q38

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[[Image:1q38.gif|left|200px]]<br /><applet load="1q38" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1q38.gif|left|200px]]
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caption="1q38" />
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'''Anastellin'''<br />
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{{Structure
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|PDB= 1q38 |SIZE=350|CAPTION= <scene name='initialview01'>1q38</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= FN1 OR FN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Anastellin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Q38 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=1Q38 OCA].
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1Q38 is a [[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=1Q38 OCA].
==Reference==
==Reference==
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Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors., Briknarova K, Akerman ME, Hoyt DW, Ruoslahti E, Ely KR, J Mol Biol. 2003 Sep 5;332(1):205-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12946358 12946358]
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Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors., Briknarova K, Akerman ME, Hoyt DW, Ruoslahti E, Ely KR, J Mol Biol. 2003 Sep 5;332(1):205-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12946358 12946358]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: amyloid fibril]]
[[Category: amyloid fibril]]
[[Category: anastellin]]
[[Category: anastellin]]
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[[Category: chaps]]
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[[Category: chap]]
[[Category: conformational exchange]]
[[Category: conformational exchange]]
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[[Category: dynamic fluctuations]]
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[[Category: dynamic fluctuation]]
[[Category: extracellular matrix]]
[[Category: extracellular matrix]]
[[Category: fibronectin type 3 (fn3) domain]]
[[Category: fibronectin type 3 (fn3) domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:32:22 2008''

Revision as of 11:32, 20 March 2008


PDB ID 1q38

Drag the structure with the mouse to rotate
Gene: FN1 OR FN (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Anastellin


Contents

Overview

Anastellin is a carboxy-terminal fragment of the first FN3 domain from human fibronectin. It is capable of polymerizing fibronectin in vitro, and it displays anti-tumor, anti-metastatic and anti-angiogenic properties in vivo. We have determined the structure of anastellin using nuclear magnetic resonance spectroscopy and identified residues critical for its activity. Anastellin exhibits dynamic fluctuations and conformational exchange in solution. Its overall topology is very similar to the corresponding region of full-length FN3 domains. However, its hydrophobic core becomes solvent-accessible and some of its beta-strands lose their protection against hydrogen bonding to beta-strands from other molecules. These features seem to be relevant for the fibronectin polymerization activity of anastellin and resemble the characteristics of amyloid fibril precursors. We suggest that this analogy is not random and may reflect similarities between fibronectin and amyloid fibril formation.

Disease

Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]

About this Structure

1Q38 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors., Briknarova K, Akerman ME, Hoyt DW, Ruoslahti E, Ely KR, J Mol Biol. 2003 Sep 5;332(1):205-15. PMID:12946358

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