1ci5
From Proteopedia
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| - | [[Image:1ci5.jpg|left|200px]] | + | [[Image:1ci5.jpg|left|200px]] |
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| - | '''GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)''' | + | {{Structure |
| + | |PDB= 1ci5 |SIZE=350|CAPTION= <scene name='initialview01'>1ci5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CI5 is a [ | + | 1CI5 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=1CI5 OCA]. |
==Reference== | ==Reference== | ||
| - | Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies., Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G, EMBO J. 1999 Jun 1;18(11):2941-9. PMID:[http:// | + | Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies., Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G, EMBO J. 1999 Jun 1;18(11):2941-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10357807 10357807] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin superfamily v-set domain]] | [[Category: immunoglobulin superfamily v-set domain]] | ||
| - | ''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 10:24:39 2008'' |
Revision as of 08:24, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)
Overview
A general strategy is presented here for producing glycan-free forms of glycoproteins without loss of function by employing apolar-to-polar mutations of surface residues in functionally irrelevant epitopes. The success of this structure-based approach was demonstrated through the expression in Escherichia coli of a soluble 11 kDa adhesion domain extracted from the heavily glycosylated 55 kDa human CD58 ectodomain. The solution structure was subsequently determined and binding to its counter-receptor CD2 studied by NMR. This mutant adhesion domain is functional as determined by several experimental methods, and the size of its binding site has been probed by chemical shift perturbations in NMR titration experiments. The new structural information supports a 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C" faces of both CD2 and CD58 adhesion domains. The region responsible for binding specificity is most likely localized on the C, C' and C" strands and the C-C' and C'-C" loops on CD58.
About this Structure
1CI5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies., Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G, EMBO J. 1999 Jun 1;18(11):2941-9. PMID:10357807
Page seeded by OCA on Thu Mar 20 10:24:39 2008
