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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.

Original publication

DOI

10.1093/emboj/18.6.1468

Type

Journal article

Journal

EMBO J

Publication Date

15/03/1999

Volume

18

Pages

1468 - 1479

Keywords

Amino Acid Sequence, Binding Sites, Computer Graphics, Crystallography, X-Ray, Fibronectins, Heparin, Humans, Integrin alpha4beta1, Integrins, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Structure, Secondary, Receptors, Lymphocyte Homing, Recombinant Proteins, Repetitive Sequences, Amino Acid, Sequence Alignment, Sequence Homology, Amino Acid, Software