The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV).
Cells interact with type IV collagen mainly via the integrins alpha 1 beta 1 and alpha 2 beta 1. A triple helical CNBr derived fragment CB3[IV], which contains the recognition sites for both integrins, was isolated from type IV collagen. Trypsin treatment of CB3[IV] gave rise to four smaller fragments, F1-F4, of which the smallest one, F4, contained the recognition site for alpha 1 beta 1. Further fragmentation of F4 by thermolysin treatment at 50 degrees C led to fragment TL1, which represents the C-terminal half of F4, and which was no longer able to interact with alpha 1 beta 1. Therefore the recognition site of alpha 1 beta 1 had to be located within the N-terminal half of F4, a position which was verified by electron micrographs of a crosslinked F2-alpha 1 beta 1 complex. Modification of the Arg and Asp residues, which abolished the binding activity of F4, led to the identification of Arg (461) within the alpha 2(IV) and Asp (461) within the alpha 1 (IV) chain as essential residues for the alpha 1 beta 1. The array of these two residues on the surface of the triple helix is discussed.
Eble
J A
JA
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Golbik
R
R
Mann
K
K
Kühn
K
K
D000595:Amino Acid Sequence; D001120:Arginine / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism; D001485:Basement Membrane / Q000378:metabolism*; D015153:Blotting, Western; D003094:Collagen / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D013696:Temperature; D013820:Thermolysin / Q000378:metabolism
D016023:Integrins; D010446:Peptide Fragments; D001224:Aspartic Acid; D003094:Collagen; D001120:Arginine; D013820:Thermolysin