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1hng
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hng OCA], [http://www.ebi.ac.uk/pdbsum/1hng PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hng RCSB]</span> | ||
}} | }} | ||
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[[Category: t lymphocyte adhesion glycoprotein]] | [[Category: t lymphocyte adhesion glycoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:58 2008'' |
Revision as of 18:07, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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