4OJK
Structure of the cGMP Dependent Protein Kinase II and Rab11b Complex
Summary for 4OJK
| Entry DOI | 10.2210/pdb4ojk/pdb |
| Related | 1ZXA 2F9L 2F9M 3NMD |
| Descriptor | Ras-related protein Rab-11B, cGMP-dependent protein kinase 2, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | small gtpase, leucine zipper, trafficking, serine/threonine kinase, membrane associated, hydrolase-protein binding complex, hydrolase/protein binding |
| Biological source | Homo sapiens (human) More |
| Cellular location | Recycling endosome membrane ; Lipid-anchor ; Cytoplasmic side : Q15907 Apical cell membrane ; Lipid-anchor : Q64595 |
| Total number of polymer chains | 4 |
| Total formula weight | 56410.66 |
| Authors | Reger, A.S.,Yang, M.P.,Guo, E.,Kim, C. (deposition date: 2014-01-21, release date: 2014-08-06, Last modification date: 2023-09-20) |
| Primary citation | 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 Cited by 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: 25070890DOI: 10.1074/jbc.M114.575894 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.657 Å) |
Structure validation
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