The EMBO Journal
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The EMBO Journal (1998) 17, 335–343, doi:10.1093/emboj/17.2.335

Figure 4
Electron microscopic structure of agrin and mapping of its binding site in laminin-1
Alain J. Denzer, Therese Schulthess, Charlotte Fauser, Beat Schumacher, Richard A. Kammerer, Jürgen Engel and Markus A. Ruegg
Figure 4
Figure 4
 The N-terminal agrin fragment binds to the three-stranded, coiled-coil domain of laminin-1. (A) Structural organization of laminin-1 (Ln) and of proteolytic fragments derived from laminin-1 by elastase treatment (E1, E3 and E8; dotted boxes) and by cathepsin G treatment (C8-9; shaded box) are shown. (B) Solid-phase radioligand-binding assay demonstrating the binding of the N-terminal agrin fragment to laminin-1 and to the fragments depicted in (A). Laminin-1 and its fragments were immobilized on microtiter plates and subsequently incubated with 5 nM [125I]cN25Fc. Each value is the mean plusminus SD of three measurements and represents binding after subtraction of the counts to bovine serum albumin-coated wells (61 plusminus 7 c.p.m.).
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