1Q38

Anastellin

Summary for 1Q38

• Entry DOI: 10.2210/pdb1q38/pdb
• Related: 1FNA 1FNF 1FNH 1J8K 2FNB
• Descriptor: Fibronectin (1 entity in total)
• Functional Keywords: amyloid fibril, anastellin, extracellular matrix, fibronectin type 3 (fn3) domain, dynamic fluctuations, conformational exchange, chaps, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751
• Total number of polymer chains: 1
• Total formula weight: 10175.41

Authors

Briknarova, K.,Akerman, M.E.,Hoyt, D.W.,Ruoslahti, E.,Ely, K.R. (deposition date: 2003-07-28, release date: 2003-11-04, Last modification date: 2024-05-22)

Primary citation

Briknarova, K.,Akerman, M.E.,Hoyt, D.W.,Ruoslahti, E.,Ely, K.R.
Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors
J.Mol.Biol., 332:205-215, 2003

PubMed Abstract: 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.

PubMed: 12946358
DOI: 10.1016/S0022-2836(03)00890-8

Experimental method

SOLUTION NMR