BINDING OF NIDOGEN AND THE LAMININ-NIDOGEN COMPLEX TO BASEMENT-MEMBRANE COLLAGEN TYPE-IV
BINDING OF NIDOGEN AND THE LAMININ-NIDOGEN COMPLEX TO BASEMENT-MEMBRANE COLLAGEN TYPE-IV
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DOI：
10.1111/j.1432-1033.1989.tb15013.x
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发表时间：
1989-09-01
期刊：
影响因子：
--
通讯作者：
TIMPL, R
中科院分区：
文献类型：
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作者：
AUMAILLEY, M;WIEDEMANN, H;TIMPL, R
固态配体结合和抑制测定表明，层粘连蛋白-巢蛋白复合物和纯化的巢蛋白均结合IV型胶原蛋白，但不结合其他胶原蛋白。从解离的复合物中纯化的层粘连蛋白和多种层粘连蛋白蛋白水解片段未能结合胶原IV。通过旋转阴影观察在巢蛋白或层粘连蛋白-巢蛋白与IV型胶原蛋白之间在溶液中形成的复合物，该复合物在距胶原蛋白三螺旋C末端约80nm的主要结合位点上进行鉴定。第二个较弱的结合位点可能更靠近其 N 末端。 nidogen 的结合位点被指定为其 C 端球状结构域，该结构域也具有层粘连蛋白结合结构。对于层粘连蛋白-巢蛋白复合物，观察到更多样化的胶原蛋白-IV 结合模式，其中相互作用可能涉及层粘连蛋白的巢蛋白和短臂结构。
The laminin-nidogen complex and purified nidogen both bind collagen IV but not other collagens, as shown by solid-state-ligand-binding and inhibition assays. Laminin purified from the dissociated complex and a variety of laminin proteolytic fragments failed to bind collagen IV. Complexes formed in solution between nidogen or laminin-nidogen and collagen IV were visualized by rotary shadowing which identified on major binding site about 80 nm away from the C-terminus of the collagen triple helix. A second, weaker binding site may exist closer to its N-terminus. Bindign sites of nidogen were assigned to its C-terminal globular domain which also possesses laminin-binding structures. A more diverse collagen-IV-binding pattern was observed for the laminin-nidogen complex, whereby interactions may involve both nidogen and short-arm structures of laminin.