3O8V

Crystal Structure of the Tudor Domains from FXR1

Summary for 3O8V

• Entry DOI: 10.2210/pdb3o8v/pdb
• Related: 3KUF
• Descriptor: Fragile X mental retardation syndrome-related protein 1 (2 entities in total)
• Functional Keywords: structural genomics consortium, sgc, tandem tudor, protein binding, rna-binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P51114
• Total number of polymer chains: 1
• Total formula weight: 15245.15

Authors

Lam, R.,Guo, Y.H.,Adams-Cioaba, M.,Bian, C.B.,Mackenzie, F.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2010-08-03, release date: 2010-08-18, Last modification date: 2024-02-21)

Primary citation

Adams-Cioaba, M.A.,Guo, Y.,Bian, C.,Amaya, M.F.,Lam, R.,Wasney, G.A.,Vedadi, M.,Xu, C.,Min, J.
Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2.
Plos One, 5:e13559-e13559, 2010

PubMed Abstract: Expansion of the CGG trinucleotide repeat in the 5'-untranslated region of the FMR1, fragile X mental retardation 1, gene results in suppression of protein expression for this gene and is the underlying cause of Fragile X syndrome. In unaffected individuals, the FMRP protein, together with two additional paralogues (Fragile X Mental Retardation Syndrome-related Protein 1 and 2), associates with mRNA to form a ribonucleoprotein complex in the nucleus that is transported to dendrites and spines of neuronal cells. It is thought that the fragile X family of proteins contributes to the regulation of protein synthesis at sites where mRNAs are locally translated in response to stimuli.

PubMed: 21072162
DOI: 10.1371/journal.pone.0013559

Experimental method

X-RAY DIFFRACTION (2.5 Å)