1hng
From Proteopedia
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| - | [[Image:1hng.jpg|left|200px]] | + | [[Image:1hng.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2''' | + | {{Structure |
| + | |PDB= 1hng |SIZE=350|CAPTION= <scene name='initialview01'>1hng</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HNG is a [ | + | 1HNG is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1279440 1279440] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:20 2008'' |
Revision as of 09:39, 20 March 2008
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| , resolution 2.8Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 11:39:20 2008
