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Crystal Structure of Foxp2 bound Specifically to DNA New Article

spinqualitylabelsall models PDB ID 2a07 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2a07, resolution 1.90Å ()
Ligands:
Gene:	FOXP2, CAGH44, TNRC10 (Homo sapiens)
Structural annotation: Resources: InterPro : Ipr001766, Ipr015880, Ipr011991, Ipr007087 Pfam : PF00250 UniProt : O15409
Functional annotation: Cellular component: intracellular nucleus Biological process: transcription putamen development regulation of transcription, DNA-dependent caudate nucleus development Molecular function: sequence-specific DNA binding metal ion binding zinc ion binding protein homodimerization activity transcription factor activity nucleic acid binding DNA binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Introduction 2 Evolutionary Conservation 3 DNA Binding 4 Domain Swapping 5 Disease Mutations 5.1 Arg553His Mutation 5.2 Ile363Val Mutation 5.3 Ala385Thr Mutation 5.4 Arg397Trp Mutation 5.5 Phe371Cys and Phe371Leu Mutations 6 References

Introduction

Evolutionary Conservation

DNA Binding

Domain Swapping

Disease Mutations

Disease mutations in FOXP2 and related proteins correspond to either the domain-swapping dimer interface or the DNA binding sequence. FOXP2 and FOXP3 are similar enough that the crystal structure of one can be used to explain the effects of mutation on structure in the other.

Arg553His Mutation

This is the only mutation that has been characterized in the original FOXP2 protein.

Ile363Val Mutation

Ala385Thr Mutation

Arg397Trp Mutation

Phe371Cys and Phe371Leu Mutations

References

• Stroud JC, Wu Y, Bates DL, Han A, Nowick K, Paabo S, Tong H, Chen L. Structure of the forkhead domain of FOXP2 bound to DNA. Structure. 2006 Jan;14(1):159-66. PMID:16407075 doi:10.1016/j.str.2005.10.005