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4P7I

Crystal structure of the Merlin FERM/DCAF1 complex

Summary for 4P7I
Entry DOI10.2210/pdb4p7i/pdb
DescriptorMerlin, Protein VPRBP, GLYCEROL, ... (4 entities in total)
Functional Keywordssignaling protein-protein binding complex, signaling protein/protein binding
Biological sourceMus musculus (Mouse)
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Cellular locationCell membrane ; Peripheral membrane protein ; Cytoplasmic side : P46662
Cytoplasm: Q9Y4B6
Total number of polymer chains4
Total formula weight88942.31
Authors
Wei, Z.,Li, Y.,Zhang, M. (deposition date: 2014-03-27, release date: 2014-04-09, Last modification date: 2023-09-27)
Primary citationLi, Y.,Wei, Z.,Zhang, J.,Yang, Z.,Zhang, M.
Structural basis of the binding of Merlin FERM domain to the E3 ubiquitin ligase substrate adaptor DCAF1.
J.Biol.Chem., 289:14674-14681, 2014
Cited by
PubMed Abstract: The tumor suppressor gene Nf2 product, Merlin, plays vital roles in controlling proper development of organ sizes by specifically binding to a large number of target proteins localized both in cytoplasm and nuclei. The FERM domain of Merlin is chiefly responsible for its binding to target proteins, although the molecular basis governing these interactions are poorly understood due to lack of structural information. Here, we report the crystal structure of the Merlin FERM domain in complex with its binding domain derived from the E3 ubiquitin ligase substrate adaptor DCAF1 (also known as VPRBP). Unlike target binding modes found in ERM proteins, the Merlin-FERM binding domain of DCAF1 folds as a β-hairpin and binds to the α1/β5-groove of the F3 lobe of Merlin-FERM via extensive hydrophobic interactions. In addition to providing the first structural glimpse of a Merlin-FERM·target complex, the structure of the Merlin·DCAF1 complex is likely to be valuable for understanding the interactions of Merlin with its binding partners other than DCAF1.
PubMed: 24706749
DOI: 10.1074/jbc.M114.551184
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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