1QGB

SOLUTION STRUCTURE OF THE N-TERMINAL F1 MODULE PAIR FROM HUMAN FIBRONECTIN

Summary for 1QGB

• Entry DOI: 10.2210/pdb1qgb/pdb
• Descriptor: PROTEIN (FIBRONECTIN) (1 entity in total)
• Functional Keywords: fibronectin type 1 module pair, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751
• Total number of polymer chains: 1
• Total formula weight: 10524.67

Authors

Potts, J.R.,Bright, J.R.,Bolton, D.,Pickford, A.R.,Campbell, I.D. (deposition date: 1999-04-21, release date: 1999-12-08, Last modification date: 2024-10-30)

Primary citation

Potts, J.R.,Bright, J.R.,Bolton, D.,Pickford, A.R.,Campbell, I.D.
Solution structure of the N-terminal F1 module pair from human fibronectin.
Biochemistry, 38:8304-8312, 1999

PubMed Abstract: 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.

PubMed: 10387076
DOI: 10.1021/bi990202b

Experimental method

SOLUTION NMR