1gya
From Proteopedia
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| - | [[Image:1gya.gif|left|200px]] | + | [[Image:1gya.gif|left|200px]] |
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| - | '''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2''' | + | {{Structure |
| + | |PDB= 1gya |SIZE=350|CAPTION= <scene name='initialview01'>1gya</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= SCD2=182= ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GYA is a [ | + | 1GYA 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=1GYA OCA]. |
==Reference== | ==Reference== | ||
| - | Conformation and function of the N-linked glycan in the adhesion domain of human CD2., Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G, Science. 1995 Sep 1;269(5228):1273-8. PMID:[http:// | + | Conformation and function of the N-linked glycan in the adhesion domain of human CD2., Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G, Science. 1995 Sep 1;269(5228):1273-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7544493 7544493] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[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 11:29:35 2008'' |
Revision as of 09:29, 20 March 2008
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| Gene: | SCD2=182= (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2
Overview
The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N-acetylglucosamine)2-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2.
About this Structure
1GYA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformation and function of the N-linked glycan in the adhesion domain of human CD2., Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G, Science. 1995 Sep 1;269(5228):1273-8. PMID:7544493
Page seeded by OCA on Thu Mar 20 11:29:35 2008
