2ems: Difference between revisions

Revision as of 13:10, 17 September 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:2ems.png

Template:STRUCTURE 2ems

Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43

Template:ABSTRACT PUBMED 18614175

About this StructureAbout this Structure

2EMS is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, J Mol Biol. 2008 Sep 5;381(3):634-44. Epub 2008 Jun 7. PMID:18614175

Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):49-51. Epub 2006 Dec 22. PMID:17183174

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OCA

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-[[Image:2ems.jpg|left|200px]]
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-'''Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43'''
+===Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43===
-==Overview==
+<!--
-Radixin is a member of the ERM proteins that cross-link plasma membranes and actin filaments. The FERM domains located in the N-terminal regions of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. Here, crystals of the radixin FERM domain bound to the cytoplasmic peptides of two adhesion molecules, CD43 and PSGL-1, have been obtained. Crystals of the radixin FERM domain bound to CD43 belong to space group P4(3)22, with unit-cell parameters a = b = 68.72, c = 201.39 A, and contain one complex in the crystallographic asymmetric unit. Crystals of the radixin FERM domain bound to PSGL-1 belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 A, and contain two complexes in the crystallographic asymmetric unit. Intensity data sets were collected to a resolution of 2.9 A for the FERM-CD43 complex and 2.8 A for the FERM-PSGL-1 complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_18614175}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18614175 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18614175}}
 ==About this Structure==
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 ==Reference==
+Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, J Mol Biol. 2008 Sep 5;381(3):634-44. Epub 2008 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18614175 18614175]
 Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):49-51. Epub 2006 Dec 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17183174 17183174]
 [[Category: Mus musculus]]
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 [[Category: Cell adhesion]]
 [[Category: Protein-peptide complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 02:48:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 17 13:10:41 2008''