期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 332, 期 1, 页码 205-215出版社
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(03)00890-8
关键词
amyloid fibril; anastellin; extracellular matrix; fibronectin type 3 (FN3) domain; NMR
资金
- NCI NIH HHS [1R41 CA82713, CA88420, 5 P30 CA30199] Funding Source: Medline
- PHS HHS [5 P01 82713-03] Funding Source: Medline
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. (C) 2003 Elsevier Ltd. All rights reserved.
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