1VA1: Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 1)

Citation:
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.
PDB ID: 1VA1Download
MMDB ID: 31863
PDB Deposition Date: 2004/2/7
Updated in MMDB: 2012/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1VA1
Label Count Molecule
Protein (1 molecule)
1
Transcription Factor SP1(Gene symbol: SP1)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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