1va2
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(New page: 200px<br /> <applet load="1va2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1va2" /> '''Solution Structure of Transcription Factor ...)
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Revision as of 17:36, 12 November 2007
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Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 2)
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hepatic venoocclusive disease with immunodeficiency OMIM:[604457], Mycobacterium tuberculosis, susceptibility to OMIM:[604457]
About this Structure
1VA2 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
NMR structure of transcription factor Sp1 DNA binding domain., Oka S, Shiraishi Y, Yoshida T, Ohkubo T, Sugiura Y, Kobayashi Y, Biochemistry. 2004 Dec 28;43(51):16027-35. PMID:15609997
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