The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily

被引：35

作者：

Brissett, NC ^{[1
]}

Perkins, SJ ^{[1
]}

机构：

[1] ROYAL FREE HOSP,SCH MED,DEPT BIOCHEM & MOLEC BIOL,LONDON NW3 2PF,ENGLAND

来源：

FEBS LETTERS | 1996年 / 388卷 / 2-3期

基金：

英国惠康基金;

关键词：

proteoglycan tandem repeat; hyaluronate; link protein; Aggrecan; C-type lectin; CD44; secondary structure prediction; protein fold recognition;

D O I：

10.1016/0014-5793(96)00576-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 moth 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.

引用

页码：211 / 216

页数：6

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