2VZD

Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex with paxillin LD1 motif

2VZD の概要

• エントリーDOI: 10.2210/pdb2vzd/pdb
• 関連するPDBエントリー: 1KKY 1KL0 2VZC 2VZG 2VZI
• 分子名称: ALPHA-PARVIN, PAXILLIN, TRIETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: calponin homology domain, cell membrane, cell adhesion, metal-binding, cytoskeleton, cell junction, actin-binding, phosphoprotein, membrane, ld1 motif, lim domain
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cell junction, focal adhesion: Q9NVD7; Cytoplasm, cytoskeleton: P49023
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36065.09

構造登録者

Lorenz, S.,Vakonakis, I.,Lowe, E.D.,Campbell, I.D.,Noble, M.E.M.,Hoellerer, M.K. (登録日: 2008-07-31, 公開日: 2008-10-28, 最終更新日: 2023-12-13)

主引用文献

Lorenz, S.,Vakonakis, I.,Lowe, E.D.,Campbell, I.D.,Noble, M.E.M.,Hoellerer, M.K.
Structural Analysis of the Interactions between Paxillin Ld Motifs and Alpha-Parvin
Structure, 16:1521-, 2008

PubMed Abstract: The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as alpha-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal structures with these LD motifs reveal the molecular details of their interactions with a common binding site on alpha-parvin-CH(C), which is located at the rim of the canonical fold and includes part of the inter-CH domain linker. Surprisingly, this binding site can accommodate LD motifs in two antiparallel orientations. Taken together, these results reveal an unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell.

PubMed: 18940607
DOI: 10.1016/J.STR.2008.08.007

実験手法

X-RAY DIFFRACTION (2.1 Å)