2mam

Solution structure of the interdigitated double Tudor domain of RBBP1

spinqualitylabelsall models 2mam Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mam is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2lcd. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ARI4A_HUMAN Interacts with the viral protein-binding domain of the retinoblastoma protein. Publication Abstract from PubMed Retinoblastoma-binding protein 1 (RBBP1) is a tumor and leukemia suppressor which binds both methylated histone tails and DNA. Our previous studies indicated that RBBP1 possesses a Tudor domain which cannot bind histone marks. In order to clarify the function of the Tudor domain, the solution structure of the RBBP1 Tudor domain was determined by NMR and is presented here. Although the proteins are unrelated, the RBBP1 Tudor domain forms an interdigitated double Tudor structure similar to the Tudor domain of JMJD2A, which is an epigenetic mark reader. This indicates the functional diversity of Tudor domains. The RBBP1 Tudor domain structure has a significant area of positively charged surface which reveals a capability of the RBBP1 Tudor domain to bind nucleic acids. NMR titration and isothermal titration calorimetry experiments indicate that the RBBP1 Tudor domain binds both double and single stranded DNA with an affinity of 10 ~ 100 muM; no apparent DNA sequence specificity was detected. The DNA binding mode and key interaction residues were analyzed in detail based on a model structure of the Tudor domain-dsDNA complex, built by HADDOCK docking using the NMR data. Electrostatic interactions mediate the binding of the Tudor domain with DNA, which is consistent with NMR experiments performed at high salt concentration. The DNA-binding residues are conserved in Tudor domains of the RBBP1 protein family, resulting in conservation of the DNA-binding function in the RBBP1 Tudor domains. Our results provide further insights into the structure and function of RBBP1. Retinoblastoma-binding protein 1 has an interdigitated double Tudor domain with DNA-binding activity.,Gong W, Wang J, Perrett S, Feng Y J Biol Chem. 2013 Dec 30. PMID:24379399 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinoblastoma-binding protein 3D structures

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