The PAX3 Paired Domain and Homeodomain Function as a Single Binding Module In Vivo to Regulate Subnuclear Localization and Mobility by a Mechanism That Requires Base-Specific Recognition

Author:

Corry Gareth N.,Raghuram Nikhil,Missiaen Kristal K.,Hu Ninghe,Hendzel Michael J.,Underhill D. Alan

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference89 articles.

1. Genetic and biochemical diversity in the Pax gene family;Underhill;Biochem. Cell Biol.,2000

2. Getting your Pax straight: Pax proteins in development and disease;Chi;Trends Genet.,2002

3. DNA sequence recognition by Pax proteins: bipartite structure of the paired domain and its binding site;Czerny;Genes Dev.,1993

4. Crystal structure of the human Pax6 paired domain–DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding;Xu;Genes Dev.,1999

5. Pax3 target gene recognition occurs through distinct modes that are differentially affected by disease-associated mutations;Corry;Pigment Cell Res.,2005

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