1cdb: Difference between revisions

Revision as of 20:35, 30 June 2008

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File:1cdb.png

Template:STRUCTURE 1cdb

STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2

Template:ABSTRACT PUBMED 7915183

About this StructureAbout this Structure

1CDB is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2., Withka JM, Wyss DF, Wagner G, Arulanandam AR, Reinherz EL, Recny MA, Structure. 1993 Sep 15;1(1):69-81. PMID:7915183

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OCA

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-'''STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2'''
+===STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2===
-==Overview==
+<!--
-BACKGROUND: CD2, a T-cell specific surface glycoprotein, is critically important for mediating adherence of T cells to antigen-presenting cells or target cells. Domain 1 of human CD2 is responsible for cell adhesion, binding to CD58 (LFA-3) expressed on the cell to which the T cell binds. Human CD2 domain 1 requires N-linked carbohydrate to maintain its native conformation and ability to bind CD58. In contrast, rat CD2 does not require N-linked carbohydrate, and binds to a different ligand, CD48. RESULTS: The three-dimensional structure of the glycosylated form of domain 1 of human CD2 has been determined by NMR spectroscopy. The overall structure resembles the typical beta-barrel of an immunoglobulin variable domain. Nuclear Overhauser enhancement contacts between the protein and the N-linked glycan have been tentatively identified. CONCLUSION: Based on our results, we propose a model showing how the N-linked glycan might be positioned in the human CD2 domain 1 structure. The model provides an explanation for the observed instability of deglycosylated human CD2, and allows residues that are important for CD58 binding to be differentiated from those affecting conformational stability via interactions with the glycan.
+The line below this paragraph, {{ABSTRACT_PUBMED_7915183}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7915183 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7915183}}
 ==About this Structure==
-CDB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDB OCA].
+CDB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDB OCA].
 ==Reference==
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 [[Category: Wyss, D F.]]
 [[Category: T lymphocyte adhesion glycoprotein]]
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