2i1k: Difference between revisions

Revision as of 05:32, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2i1k.png

Template:STRUCTURE 2i1k

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

Template:ABSTRACT PUBMED 17134719

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 05:32:09 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17134719}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17134719 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17134719}}
 ==About this Structure==
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 [[Category: Regulation]]
 [[Category: Self-inhibition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:57:56 2008''
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