1VA2

Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 2)

Summary for 1VA2

• Entry DOI: 10.2210/pdb1va2/pdb
• Related: 1VA1 1VA3
• Descriptor: Transcription factor Sp1, ZINC ION (2 entities in total)
• Functional Keywords: c2h2 type zinc finger, transcription factor, dna-binding protein, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P08047
• Total number of polymer chains: 1
• Total formula weight: 3918.83

Authors

Oka, S.,Shiraishi, Y.,Yoshida, T.,Ohkubo, T.,Sugiura, Y.,Kobayashi, Y. (deposition date: 2004-02-07, release date: 2005-02-08, Last modification date: 2023-12-27)

Primary citation

Oka, S.,Shiraishi, Y.,Yoshida, T.,Ohkubo, T.,Sugiura, Y.,Kobayashi, Y.
NMR structure of transcription factor Sp1 DNA binding domain
Biochemistry, 43:16027-16035, 2004

PubMed Abstract: To understand the DNA recognition mechanism of zinc finger motifs of transcription factor Sp1, we have determined the solution structure of DNA-binding domain of the Sp1 by solution NMR techniques. The DNA-binding domain of Sp1 consists of three Cys(2)His(2)-type zinc finger motifs. They have typical betabetaalpha zinc finger folds and relatively random orientations. From DNA-binding analysis performed by NMR and comparison between structures determined here and previously reported structures of other zinc fingers, it was assumed that DNA recognition modes of fingers 2 and 3 would be similar to those of fingers of Zif268, in which each finger recognizes four base pairs strictly by using residues at positions -1, 2, 3, and 6 of the recognition helix. On the contrary, finger 1 can use only two residues for DNA recognition, Lys550 and His553 at positions -1 and 3 of the helix, and has more relaxed sequence and site specificity than other Cys(2)His(2) zinc fingers. It is proposed that this relaxed property of finger 1 allows transcription factor Sp1 to bind various DNA sequences with high affinity.

PubMed: 15609997
DOI: 10.1021/bi048438p

Experimental method

SOLUTION NMR