2D2Z

Crystal structure of Soluble Form Of CLIC4

Summary for 2D2Z

• Entry DOI: 10.2210/pdb2d2z/pdb
• Descriptor: Chloride intracellular channel protein 4 (2 entities in total)
• Functional Keywords: soluble form, clic4, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome: Q9Y696
• Total number of polymer chains: 3
• Total formula weight: 89640.74

Authors

Li, Y.F.,Li, D.F.,Wang, D.C. (deposition date: 2005-09-21, release date: 2006-05-16, Last modification date: 2024-03-13)

Primary citation

Li, Y.F.,Li, D.F.,Zeng, Z.H.,Wang, D.C.
Trimeric structure of the wild soluble chloride intracellular ion channel CLIC4 observed in crystals
Biochem.Biophys.Res.Commun., 343:1272-1278, 2006

PubMed Abstract: The crystal structure of a wild type of the human soluble chloride intracellular ion channel CLIC4 (wCLIC4) has been determined at a resolution of 2.2A. The structure shows a homotrimer in an asymmetric unit, which is first observed in CLICs. The assembly of the trimer takes a unique triple interaction mode between three monomers with a hydrogen-bond network and hydrophobic contacts. Through such complicated interactions, the homotrimer of wCLIC4 is firmly stabilized. The structure shows an oligomeric mode with a unique assembly mechanism by which the oligomerization of CLIC4 can be performed without any intramolecular disulfide bond formation. It indicated a possibility that CLIC4 may take a unique structural organization distinct from CLIC1 for docking with lipid bilayers. In addition, the structure shows distinct conformational states of the h2 region for respective monomers of the trimer, which reveal an intrinsic conformational susceptibility for this significant region in the structural transition.

PubMed: 16581025
DOI: 10.1016/j.bbrc.2006.03.099

Experimental method

X-RAY DIFFRACTION (2.2 Å)