Novel interaction partners of the CD2BP2-GYF domain

被引：19

作者：

Kofler, M

Motzny, K

Beyermann, M

Freund, C

机构：

[1] Forschungsinst Mol Pharmakol, Prot Engn Grp, D-13125 Berlin, Germany

[2] Free Univ Berlin, D-13125 Berlin, Germany

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2005年 / 280卷 / 39期

关键词：

D O I：

10.1074/jbc.M503989200

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：

The GYF domain of CD2BP2 serves as an adapter that recognizes proline-rich sequences in intracellular proteins. Although the T cell adhesion molecule CD2 and the core splicing protein SmB/B' were previously shown to interact with CD2BP2-GYF, we are now using a general approach to identify putative GYF domain target sites within the human proteome. The phage display-derived recognition motif for CD2BP2-GYF is PPG(W/F/Y/M/L). SPOT analysis confirmed that the GYF domain interacts with peptides from human proteins containing the consensus site. Epitope mapping by NMR spectroscopy performed for several peptides revealed a conserved binding surface. A direct interaction of the CD2BP2-GYF domain with the novel protein interaction partners PI31 and NPWBP was verified by yeast two-hybrid analysis.

引用

收藏

页码：33397 / 33402

页数：6

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