1FNH

CRYSTAL STRUCTURE OF HEPARIN AND INTEGRIN BINDING SEGMENT OF HUMAN FIBRONECTIN

Summary for 1FNH

• Entry DOI: 10.2210/pdb1fnh/pdb
• Descriptor: PROTEIN (FIBRONECTIN) (2 entities in total)
• Functional Keywords: heparin and integrin binding
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751
• Total number of polymer chains: 1
• Total formula weight: 29625.73

Authors

Sharma, A.,Askari, J.,Humphries, M.,Jones, E.Y.,Stuart, D.I. (deposition date: 1999-01-28, release date: 1999-03-16, Last modification date: 2023-12-27)

Primary citation

Sharma, A.,Askari, J.A.,Humphries, M.J.,Jones, E.Y.,Stuart, D.I.
Crystal structure of a heparin- and integrin-binding segment of human fibronectin.
EMBO J., 18:1468-1479, 1999

PubMed Abstract: The crystal structure of human fibronectin (FN) type III repeats 12-14 reveals the primary heparin-binding site, a clump of positively charged residues in FN13, and a putative minor site approximately 60 A away in FN14. The IDAPS motif implicated in integrin alpha4beta1 binding is at the FN13-14 junction, rendering the critical Asp184 inaccessible to integrin. Asp184 clamps the BC loop of FN14, whose sequence (PRARI) is reminiscent of the synergy sequence (PHSRN) of FN9. Mutagenesis studies prompted by this observation reveal that both arginines of the PRARI sequence are important for alpha4beta1 binding to FN12-14. The PRARI motif may represent a new class of integrin-binding sites. The spatial organization of the binding sites suggests that heparin and integrin may bind in concert.

PubMed: 10075919
DOI: 10.1093/emboj/18.6.1468

Experimental method

X-RAY DIFFRACTION (2.8 Å)