1sp1

From Proteopedia

Revision as of 13:59, 30 October 2007

NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F3, MINIMIZED AVERAGE STRUCTURE

Overview

The carboxyl terminus of transcription factor Sp1 contains three, contiguous Cys2-His2 zinc finger domains with the consensus sequence, Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear, two-dimensional NMR techniques to solve the solution structures of, synthetic peptides corresponding to the last two zinc finger domains, (Sp1f2 and Sp1f3, respectively) of Sp1. Our studies indicate a classical, Cys2-His2 type fold for both the domains differing from each other, primarily in the conformation of Cys-X2-Cys (beta-type I turn) and, Cys-X4-Cys (beta-type II turn) elements. There are, however, no, significant differences in the metal binding properties between the, Cys-X4-Cys (Sp1f2) and Cys-X2-Cys (Sp1f3) subclasses of zinc fingers. The, free solution structures of Sp1f2 and ... [(full description)]

About this Structure

1SP1 is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].

Reference

Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition., Narayan VA, Kriwacki RW, Caradonna JP, J Biol Chem. 1997 Mar 21;272(12):7801-9. PMID:9065444

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