title: High-resolution structural studies of the factor XIIIa crosslinking site and the first type 1 module of fibronectin.
abstract: The N-terminal domain of fibronectin undergoes factor XIIIa-catalysed crosslinking to fibrin, bacteria and collagen. The reactive glutamine residue is in an extended, random coil 'tail' of about 18 residues that would be accessible for crosslinking.
authors.forename: J R
authors.initials: JR
authors.lastname: Potts
authors.forename: I
authors.initials: I
authors.lastname: Phan
authors.forename: M J
authors.initials: MJ
authors.lastname: Williams
authors.forename: I D
authors.initials: ID
authors.lastname: Campbell
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D005337:Fibrin / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry* / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D011503:Transglutaminases / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D005353:Fibronectins; D010446:Peptide Fragments; D005973:Glutamine; D005337:Fibrin; D003094:Collagen; D011503:Transglutaminases