User:Eran Hodis/Sandbox3

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==Your Heading Here (maybe something like 'Structure')==
==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='1dq8' size='200' structureSide='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' text='The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical DNA wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility.' />
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<StructureSection load='1dq8' size='200' structureSide='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])'
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text='
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The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical DNA wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility.
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Revision as of 17:12, 31 October 2010

Contents

Your Heading Here (maybe something like 'Structure')

Structure of HMG-CoA reductase (PDB entry 1dq8)

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PDB ID 1aoi

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Nucleosome Structure

PDB ID 1aoi

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Introduction

The nucleosome core particle contains two copies of each histone protein (H2A, H2B, H3 and H4) and 146 basepairs (bp) of superhelical DNA wrapped around this histone octamer. It represents the first order of DNA packaging in the nucleus and as such is the principal structure that determines DNA accessibility.

The Histone Octamer


Two copies of each histone protein, H2A, H2B, H3, and H4, are assembled into an octameric disc. Although each monomer has an N-terminal tail that projects from the histone core, the structure at left shows only a single tail from one H3 monomer.


All four histone proteins share a highly similar structural motif, the histone fold, comprising three alpha helices connected by two loops (shown here for H2A):

alpha1-loop1-alpha2-loop2-alpha3

Proteopedia Page Contributors and Editors (what is this?)

Eran Hodis

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