User:Liz Thomas/Sandbox 1

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(New page: {|style="width:100%; border:1px solid #E1A524; margin-top=1.0em; background: #99CCFF" | | <div style="font-size:175%; padding-top:0.5em; padding-left:30.0px;">Crystal Structure of Foxp2 bo...)
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{{STRUCTURE_2a07| PDB=2a07 | SCENE= }}
{{STRUCTURE_2a07| PDB=2a07 | SCENE= }}
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==Introduction==
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==Evolutionary Conservation==
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==DNA Binding==
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==Domain Swapping==
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==Disease Mutations==
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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.
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'''Arg553His Mutation'''<br>
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This is the only mutation that has been characterized in the original FOXP2 protein.
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'''Ile363Val Mutation'''
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'''Ala385Thr Mutation'''
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'''Arg397Trp Mutation'''
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'''Phe371Cys and Phe371Leu Mutations'''

Revision as of 21:24, 10 March 2010

Crystal Structure of Foxp2 bound Specifically to DNA
New Article


PDB ID 2a07

Drag the structure with the mouse to rotate
2a07, resolution 1.90Å ()
Ligands:
Gene: FOXP2, CAGH44, TNRC10 (Homo sapiens)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

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

Proteopedia Page Contributors and Editors (what is this?)

Liz Thomas

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