Brissett N C, Perkins S J
Department of Biochemistry and Molecular Biology, Royal Free Hospital School of Medicine, London, UK.
FEBS Lett. 1996 Jun 17;388(2-3):211-6. doi: 10.1016/0014-5793(96)00576-5.
Link protein and aggrecan of the extracellular matrix each contain two proteoglycan tandem repeat (PTR) domains that interact with hyaluronate. Consensus secondary structure predictions for 59 PTR sequences and 129 C-type lectin sequences give similar patterns of two alpha-helices and up to seven beta-strands. Protein fold recognition analyses show that the 59 PTR sequences are highly compatible with the C-type lectin crystal structure. The predicted fold consists of a conserved motif formed from an antiparallel beta-sheet flanked by two alpha-helices, the motif being attached to two distinct types of beta-sheet region in the two superfamilies. Arg9 or Lys11 on an exposed loop and up to three other Arg residues in the beta-sheet region are conserved and may form part of a hyaluronate binding site.
细胞外基质中的连接蛋白和聚集蛋白聚糖各自包含两个与透明质酸相互作用的蛋白聚糖串联重复（PTR）结构域。对59个PTR序列和129个C型凝集素序列的共有二级结构预测给出了两个α螺旋和多达七个β链的相似模式。蛋白质折叠识别分析表明，59个PTR序列与C型凝集素晶体结构高度兼容。预测的折叠结构由一个由反平行β折叠侧翼的两个α螺旋形成的保守基序组成，该基序连接到两个超家族中两种不同类型的β折叠区域。暴露环上的精氨酸9或赖氨酸11以及β折叠区域中多达三个其他精氨酸残基是保守的，可能构成透明质酸结合位点的一部分。
