2KK0

Solution structure of dead ringer-like protein 1 (at-rich interactive domain-containing protein 3a) from homo sapiens, northeast structural genomics consortium (NESG) target hr4394c

Summary for 2KK0

• Entry DOI: 10.2210/pdb2kk0/pdb
• NMR Information: BMRB: 16348
• Descriptor: AT-rich interactive domain-containing protein 3A (1 entity in total)
• Functional Keywords: dead ringer, at-rich interaction domain, nesg, arid, cytoplasm, dna-binding, nucleus, phosphoprotein, polymorphism, transcription, transcription regulation, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, transcription regulator
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17162.66

Authors

Liu, G.,Wang, D.,Nwosu, C.,Owens, L.,Xiao, R.,Liu, J.,Baran, M.C.,Swapna, G.,Acton, T.B.,Rost, B.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2009-06-14, release date: 2009-07-14, Last modification date: 2024-05-08)

Primary citation

Liu, G.,Huang, Y.J.,Xiao, R.,Wang, D.,Acton, T.B.,Montelione, G.T.
Solution NMR structure of the ARID domain of human AT-rich interactive domain-containing protein 3A: a human cancer protein interaction network target.
Proteins, 78:2170-2175, 2010

PubMed Abstract: The AT-rich interactive domain (ARID) of human AT-rich interactive domain-containing protein 3A (ARID3A) has been selected for structural characterization by Northeast Structural Genomics Consortium (residues 218-351 NESG ID HR4394C) as part of our Human Cancer Protein Interaction Network (HCPIN) project. Protein ARID3A belongs to the ARID family DNA-binding protein and is known to play important roles in embryonic patterning, cell lineage gene regulation, and cell cycle control, chromatin remodeling and transcriptional regulations. The solution NMR structure of ARID3A ARID domain consists of eight α-helices α0-α7 and a short β hairpin. Helix α0 and α1 form a V shape, helix α2-α4 and helix α5-α7 form two U shapes, and the V and two U shapes packed orthogonal to each other. The NMR structure of the ARID domain of human ARID3A reported here provides a structural basis for elucidating the regulatory mechanisms of ARID3A function, and the molecular mechanism of ARID3A interactions with DNA. It also has potential value in future drug discovery and design.

PubMed: 20455271
DOI: 10.1002/prot.22718

Experimental method

SOLUTION NMR