2i1k

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[[Image:2i1k.gif|left|200px]]<br /><applet load="2i1k" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2i1k.gif|left|200px]]
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caption="2i1k, resolution 3.000&Aring;" />
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'''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution'''<br />
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{{Structure
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|PDB= 2i1k |SIZE=350|CAPTION= <scene name='initialview01'>2i1k</scene>, resolution 3.000&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=URE:UREA'>URE</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2I1K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=URE:'>URE</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1K OCA].
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2I1K is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1K OCA].
==Reference==
==Reference==
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Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain., Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ, J Mol Biol. 2007 Feb 2;365(5):1446-59. Epub 2006 Oct 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17134719 17134719]
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Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain., Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ, J Mol Biol. 2007 Feb 2;365(5):1446-59. Epub 2006 Oct 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17134719 17134719]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Spodoptera frugiperda]]
[[Category: Spodoptera frugiperda]]
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[[Category: self-inhibition]]
[[Category: self-inhibition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:24:18 2008''

Revision as of 15:24, 20 March 2008

Image:2i1k.gif


PDB ID 2i1k

Drag the structure with the mouse to rotate
, resolution 3.000Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution


Overview

Ezrin/radixin/moesin (ERM) family members provide a regulated link between the cortical actin cytoskeleton and the plasma membrane to govern membrane structure and organization. Here, we report the crystal structure of intact insect moesin, revealing that its essential yet previously uncharacterized alpha-helical domain forms extensive interactions with conserved surfaces of the band four-point-one/ezrin/radixin/moesin (FERM) domain. These interdomain contacts provide a functional explanation for how PIP(2) binding and tyrosine phosphorylation of ezrin lead to activation, and provide an understanding of previously enigmatic loss-of-function missense mutations in the tumor suppressor merlin. Sequence conservation and biochemical results indicate that this structure represents a complete model for the closed state of all ERM-merlin proteins, wherein the central alpha-helical domain is an active participant in an extensive set of inhibitory interactions that can be unmasked, in a rheostat-like manner, by coincident regulatory factors that help determine cell polarity and membrane structure.

About this Structure

2I1K is a Protein complex structure of sequences from Spodoptera frugiperda. Full crystallographic information is available from OCA.

Reference

Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain., Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ, J Mol Biol. 2007 Feb 2;365(5):1446-59. Epub 2006 Oct 26. PMID:17134719

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