期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 367, 期 2, 页码 303-309出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.10.017
关键词
fibronectin; EIIIB; neovascularization; structure
资金
- NIDCR NIH HHS [R01 DE014394-05, R01 DE014394, DE-014394] Funding Source: Medline
The alternatively spliced type III extradomain B (EIIIB) of fibronectin (FN) is expressed only during embryogenesis, wound healing and tumorigenesis. The biological function of this domain is unclear. We describe here the first crystal structure of the interface between alternatively spliced EIIIB and its adjacent IN type III domain 8 (FN B-8). The opened CC' loop of EIIIB, and the rotation and tilt of EIIIB allow good access to the FG loop of FN-8, which is normally hindered by the CC' loop of FN-7. In addition, the AGEGIP sequence of the CC loop of EIIIB replaces the NGQQGN sequence of the CC' loop of FN-7. Finally, the CC loop of EIIIB forms an acidic groove with FN-8. These structural findings warrant future studies directed at identifying potential binding partners for FN B-8 interface, linking EIIIB to skeletal and cartilaginous development, wound healing, and tumorigenesis, respectively. (c) 2006 Elsevier Ltd. All rights reserved.
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