2008年10月
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP)
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
- ,
- ,
- ,
- 巻
- 64
- 号
- Pt 10
- 開始ページ
- 911
- 終了ページ
- 913
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1107/S1744309108026869
- 出版者・発行元
- BLACKWELL PUBLISHING
ERM proteins play a role in the cross-linking found between plasma membranes and actin filaments. The N-terminal FERM domains of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. During cell migration and movement, membrane-type 1 matrix metalloproteinase (MT1-MMP) on plasma membranes sheds adhesion molecule CD44 in addition to degrading the extracellular matrix. Here, the interaction between the radixin FERM domain and the MT1-MMP cytoplasmic tail is reported and preliminary crystallographic characterization of crystals of the radixin FERM domain bound to the cytoplasmic tail of MT1-MMP is presented. The crystals belong to space group P6(1)22, with unit-cell parameters a = b = 122.7, c = 128.3 angstrom, and contain one complex in the crystallographic asymmetric unit. The diffraction data were collected to a resolution of 2.4 angstrom.
- リンク情報
- ID情報
-
- DOI : 10.1107/S1744309108026869
- ISSN : 1744-3091
- PubMed ID : 18931433
- Web of Science ID : WOS:000260008100007