1vmo: Difference between revisions

Revision as of 11:48, 28 July 2008

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File:1vmo.png

Template:STRUCTURE 1vmo

CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRYCRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRY

Template:ABSTRACT PUBMED 8131734

About this StructureAbout this Structure

1VMO is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry., Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K, EMBO J. 1994 Mar 1;13(5):1003-10. PMID:8131734

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OCA

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-[[Image:1vmo.gif|left|200px]]
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-'''CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRY'''
+===CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRY===
-==Overview==
+<!--
-The crystal structure of vitelline membrane outer layer protein I (VMO-I), which is isolated from the vitelline membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I.
+The line below this paragraph, {{ABSTRACT_PUBMED_8131734}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8131734 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8131734}}
 ==About this Structure==
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 [[Category: Vassylyev, D G.]]
 [[Category: Membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:43:30 2008''
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