4OVA

Structure of the two tandem Tudor domains and a new identified KH0 domain from human Fragile X Mental Retardation Protein

Summary for 4OVA

• Entry DOI: 10.2210/pdb4ova/pdb
• Related: 2qnd
• Descriptor: Fragile X mental retardation protein 1, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: kh domain, fragile x mental retardation protein, fmrp, tandem tudor domains, eukaryotic kh domains, kh0 domain, rna binding protein, protein interaction
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q06787
• Total number of polymer chains: 4
• Total formula weight: 97495.18

Authors

Chen, Z.H.,Chen, Z.Z. (deposition date: 2014-02-21, release date: 2015-02-25, Last modification date: 2024-11-20)

Primary citation

Hu, Y.,Chen, Z.H.,Fu, Y.,He, Q.,Jiang, L.,Zheng, J.,Gao, Y.,Mei, P.,Chen, Z.Z.,Ren, X.
The amino-terminal structure of human fragile X mental retardation protein obtained using precipitant-immobilized imprinted polymers
Nat Commun, 6:6634-6634, 2015

PubMed Abstract: Flexibility is an intrinsic property of proteins and essential for their biological functions. However, because of structural flexibility, obtaining high-quality crystals of proteins with heterogeneous conformations remain challenging. Here, we show a novel approach to immobilize traditional precipitants onto molecularly imprinted polymers (MIPs) to facilitate protein crystallization, especially for flexible proteins. By applying this method, high-quality crystals of the flexible N-terminus of human fragile X mental retardation protein are obtained, whose absence causes the most common inherited mental retardation. A novel KH domain and an intermolecular disulfide bond are discovered, and several types of dimers are found in solution, thus providing insights into the function of this protein. Furthermore, the precipitant-immobilized MIPs (piMIPs) successfully facilitate flexible protein crystal formation for five model proteins with increased diffraction resolution. This highlights the potential of piMIPs for the crystallization of flexible proteins.

PubMed: 25799254
DOI: 10.1038/ncomms7634

Experimental method

X-RAY DIFFRACTION (3 Å)