1RYU
Solution Structure of the SWI1 ARID
Summary for 1RYU
Entry DOI | 10.2210/pdb1ryu/pdb |
NMR Information | BMRB: 5748 |
Descriptor | SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 (1 entity in total) |
Functional Keywords | arid, swi1, structural genomics, protein-dna interaction, dna binding protein |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: O14497 |
Total number of polymer chains | 1 |
Total formula weight | 13586.55 |
Authors | Kim, S.,Zhang, Z.,Upchurch, S.,Isern, N.,Chen, Y. (deposition date: 2003-12-22, release date: 2004-05-25, Last modification date: 2024-05-22) |
Primary citation | Kim, S.,Zhang, Z.,Upchurch, S.,Isern, N.,Chen, Y. Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition. J.Biol.Chem., 279:16670-16676, 2004 Cited by PubMed Abstract: ARID (AT-rich interaction domain) is a homologous family of DNA-binding domains that occur in DNA-binding proteins from a wide variety of species, ranging from yeast to nematodes, insects, mammals, and plants. SWI1, a member of the SWI/SNF protein complex that is involved in chromatin remodeling during transcription, contains the ARID motif. The ARID domain of human SWI1 (also known as p270) does not select for a specific DNA sequence from a random sequence pool. The lack of sequence specificity shown by the SWI1 ARID domain stands in contrast to the other characterized ARID domains, which recognize specific AT-rich sequences. We have solved the three-dimensional structure of human SWI1 ARID using solution NMR methods. In addition, we have characterized nonspecific DNA binding by the SWI1 ARID domain. Results from this study indicate that a flexible, long, internal loop in the ARID motif is likely to be important for sequence-specific DNA recognition. The structure of the human SWI1 ARID domain also represents a distinct structural subfamily. Studies of ARID indicate that the boundary of DNA binding structural and functional domains can extend beyond the sequence homologous region in a homologous family of proteins. Structural studies of homologous domains such as the ARID family of DNA-binding domains should provide information to better predict the boundary of structural and functional domains in structural genomic studies. PubMed: 14722072DOI: 10.1074/jbc.M312115200 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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