4.7 Article

Crystallographic Insight into Collagen Recognition by Discoidin Domain Receptor 2

期刊

STRUCTURE
卷 17, 期 12, 页码 1573-1581

出版社

CELL PRESS
DOI: 10.1016/j.str.2009.10.012

关键词

-

资金

  1. Wellcome Trust
  2. UK Medical Research Council
  3. BBSRC [BB/D524840/1] Funding Source: UKRI
  4. MRC [G0500707, G0701121] Funding Source: UKRI
  5. Biotechnology and Biological Sciences Research Council [BB/D524840/1] Funding Source: researchfish
  6. Medical Research Council [G0701121, G0500707] Funding Source: researchfish

向作者/读者索取更多资源

The discoidin domain receptors, DDR1 and DDR2, are widely expressed receptor tyrosine kinases that are activated by triple-helical collagen. They control important aspects of cell behavior and are dysregulated in several human diseases. The major DDR2-binding site in collagens I-III is a GVMGFO motif (O is hydroxyproline) that also binds the matricellular protein SPARC. We have determined the crystal structure of the discoidin domain of human DDR2 bound to a triple-helical collagen peptide. The GVMGFO motifs of two collagen chains are recognized by an amphiphilic pocket delimited by a functionally critical tryptophan residue and a buried salt bridge. Collagen binding results in structural changes of DDR2 surface loops that may be linked to the process of receptor activation. A comparison of the GVMGFO-binding sites of DDR2 and SPARC reveals a striking case of convergent evolution in collagen recognition.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据