1hng

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(New page: 200px<br /><applet load="1hng" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hng, resolution 2.8&Aring;" /> '''CRYSTAL STRUCTURE AT ...)
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[[Image:1hng.jpg|left|200px]]<br /><applet load="1hng" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hng, resolution 2.8&Aring;" />
caption="1hng, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2'''<br />
'''CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2'''<br />
==Overview==
==Overview==
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The crystal structure of a soluble form of the T lymphocyte antigen CD2, provides the first complete view of the extracellular region of a cell, adhesion molecule. The topology of the molecule, which comprises two, immunoglobulin-like domains, is the same as that of the first two domains, of CD4 but the relative domain orientation is altered by a fairly flexible, linker region. The putative ligand-binding beta-sheet forms a flat surface, towards the top of the molecule. Crystal contacts between these surfaces, suggest a plausible model for the adhesive interaction.
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The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.
==About this Structure==
==About this Structure==
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1HNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HNG OCA].
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1HNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNG OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davis, S.J.]]
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[[Category: Davis, S J.]]
[[Category: Harlos, K.]]
[[Category: Harlos, K.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
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[[Category: Williams, A.F.]]
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[[Category: Williams, A F.]]
[[Category: t lymphocyte adhesion glycoprotein]]
[[Category: t lymphocyte adhesion glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:40:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:04 2008''

Revision as of 11:03, 21 February 2008


1hng, resolution 2.8Å

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CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2

Overview

The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.

About this Structure

1HNG is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2., Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI, Nature. 1992 Nov 19;360(6401):232-9. PMID:1279440

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