1qgb | pdb_00001qgb
SOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM HUMAN FIBRONECTIN
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Overview
Multiple sites within the N-terminal domain (1-5F1) of fibronectin have, been implicated previously in fibronectin matrix assembly, heparin, binding, and binding to cell surface proteins of pathogenic bacteria. The, solution structure of 1F1(2)F1, the N-terminal F1 module pair from human, fibronectin, has been determined using NMR spectroscopy. Both modules in, the pair conform to the F1 consensus fold. In 4F1(5)F1, the only other F1, module pair structure available, there is a well-defined intermodule, interface; in 1F1(2)F1, however, there is no detectable interface between, the modules. Comparison of the backbone 15N-{1H} NOE values for both, module pairs confirms that the longer intermodule sequence in 1F1(2)F1 is, flexible and that the stabilization of the 4F1 C-D loop observed in, 4F1(5)F1, as a result of the intermodule interface, is not observed in, 1F1(2)F1.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
1QGB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the N-terminal F1 module pair from human fibronectin., Potts JR, Bright JR, Bolton D, Pickford AR, Campbell ID, Biochemistry. 1999 Jun 29;38(26):8304-12. PMID:10387076
Page seeded by OCA on Mon Nov 12 18:52:55 2007
