4OJK

Structure of the cGMP Dependent Protein Kinase II and Rab11b Complex

4OJK の概要

• エントリーDOI: 10.2210/pdb4ojk/pdb
• 関連するPDBエントリー: 1ZXA 2F9L 2F9M 3NMD
• 分子名称: Ras-related protein Rab-11B, cGMP-dependent protein kinase 2, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: small gtpase, leucine zipper, trafficking, serine/threonine kinase, membrane associated, hydrolase-protein binding complex, hydrolase/protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Recycling endosome membrane ; Lipid-anchor ; Cytoplasmic side : Q15907; Apical cell membrane ; Lipid-anchor : Q64595
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56410.66

構造登録者

Reger, A.S.,Yang, M.P.,Guo, E.,Kim, C. (登録日: 2014-01-21, 公開日: 2014-08-06, 最終更新日: 2023-09-20)

主引用文献

Reger, A.S.,Yang, M.P.,Koide-Yoshida, S.,Guo, E.,Mehta, S.,Yuasa, K.,Liu, A.,Casteel, D.E.,Kim, C.
Crystal Structure of the cGMP-dependent Protein Kinase II Leucine Zipper and Rab11b Protein Complex Reveals Molecular Details of G-kinase-specific Interactions.
J.Biol.Chem., 289:25393-25403, 2014

PubMed Abstract: cGMP-dependent protein kinase (PKG)-interacting proteins (GKIPs) mediate cellular targeting of PKG isoforms by interacting with their leucine zipper (LZ) domains. These interactions prevent aberrant signaling cross-talk between different PKG isotypes. To gain detailed insight into isotype-specific GKIP recognition by PKG, we analyzed the type II PKG leucine zipper domain and found that residues 40-83 dimerized and specifically interacted with Rab11b. Next, we determined a crystal structure of the PKG II LZ-Rab11b complex. The PKG II LZ domain presents a mostly nonpolar surface onto which Rab11b docks, through van der Waals interactions. Contact surfaces in Rab11b are found in switch I and II, interswitch, and the β1/N-terminal regions. This binding surface dramatically differs from that seen in the Rab11 family of interacting protein complex structures. Structural comparison with PKG Iα and Iβ LZs combined with mutagenic analysis reveals that GKIP recognition is mediated through surface charge interactions.

PubMed: 25070890
DOI: 10.1074/jbc.M114.575894

実験手法

X-RAY DIFFRACTION (2.657 Å)