1q38
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= FN1 OR FN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FN1 OR FN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fna|1FNA]], [[1fnf|1FNF]], [[1fnh|1FNH]], [[1j8k|1J8K]], [[2fnb|2FNB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q38 OCA], [http://www.ebi.ac.uk/pdbsum/1q38 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q38 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=135600 135600]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: fibronectin type 3 (fn3) domain]] | [[Category: fibronectin type 3 (fn3) domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:08:11 2008'' |
Revision as of 20:08, 30 March 2008
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| Gene: | FN1 OR FN (Homo sapiens) | ||||||
| Related: | 1FNA, 1FNF, 1FNH, 1J8K, 2FNB
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Anastellin
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.
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
Page seeded by OCA on Sun Mar 30 23:08:11 2008
