1hnf
From Proteopedia
(New page: 200px<br /> <applet load="1hnf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hnf, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="1hnf, resolution 2.5Å" /> | caption="1hnf, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HNF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HNF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: t lymphocyte adhesion glycoprotein]] | [[Category: t lymphocyte adhesion glycoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:18 2008'' |
Revision as of 13:57, 15 February 2008
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION
Overview
BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule, implicated in immune responses in vivo. The extracellular regions of the, human and rat homologues of CD2 share only 45% sequence identity and bind, different protein ligands. Comparison of the human and rat soluble CD2, (sCD2) structures should provide insights into the structural basis of, cell surface recognition. RESULTS: We therefore determined the crystal, structure of a form of human sCD2 with single N-acetylglucosamine residues, at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%., It is composed of two immunoglobulin superfamily domains similar to those, of rat sCD2, but the relative orientation of the domains in the two, homologues differs by up to 20 degrees. An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically, related human sCD2 molecules duplicates, in a different lattice, that, observed in the rat sCD2 crystals. CONCLUSIONS: Intramolecular flexibility, appears to be a conserved feature of CD2. The head-to-head interaction, between molecules represents a general model for interactions between, adhesion molecules of this structural class. Ligand specificity may be, influenced by the distribution of charged residues on the binding face.
About this Structure
1HNF is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution., Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SJ, Structure. 1994 Aug 15;2(8):755-66. PMID:7994575
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