2gk2
From Proteopedia
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==Overview== | ==Overview== | ||
| - | CEACAM1 is a cellular adhesion molecule whose protein expression is | + | CEACAM1 is a cellular adhesion molecule whose protein expression is down-regulated in several carcinomas and which also contributes to the pathogenicity of Neisseria by acting as a receptor for Opa proteins. The crystal structure of the N-terminal (D1) domain of human CEACAM1 has been determined at 2.2 Angstrom resolution. The structure shows several differences compared with a lower resolution model of the same domain from mouse solved previously, especially in the functional regions. Mapping of the sites of mutations that lower or abolish the binding of CEACAM1 to Opa proteins shows a distinct clustering of residues on the GFCC'C'' face of the molecule. Prominent amongst these are residues in the C, C' and F strands and the CC' loop. A similar analysis shows that the region responsible for homophilic or heterophilic interactions of CEACAM1 is also on the GFCC'C'' face and overlaps partially with the Opa-binding region. This higher resolution structure of CEACAM1 will facilitate a more precise dissection of its functional regions in the context of neisserial pathogenesis, cellular adhesion and immune evasion. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Davies, C.]] | [[Category: Davies, C.]] | ||
[[Category: Fedarovich, A.]] | [[Category: Fedarovich, A.]] | ||
| - | [[Category: Nicholas, R | + | [[Category: Nicholas, R A.]] |
[[Category: Tomberg, J.]] | [[Category: Tomberg, J.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: immunoglobulin domain]] | [[Category: immunoglobulin domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:33 2008'' |
Revision as of 15:32, 21 February 2008
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Crystal structure of the N terminal domain of human CEACAM1
Overview
CEACAM1 is a cellular adhesion molecule whose protein expression is down-regulated in several carcinomas and which also contributes to the pathogenicity of Neisseria by acting as a receptor for Opa proteins. The crystal structure of the N-terminal (D1) domain of human CEACAM1 has been determined at 2.2 Angstrom resolution. The structure shows several differences compared with a lower resolution model of the same domain from mouse solved previously, especially in the functional regions. Mapping of the sites of mutations that lower or abolish the binding of CEACAM1 to Opa proteins shows a distinct clustering of residues on the GFCC'C face of the molecule. Prominent amongst these are residues in the C, C' and F strands and the CC' loop. A similar analysis shows that the region responsible for homophilic or heterophilic interactions of CEACAM1 is also on the GFCC'C face and overlaps partially with the Opa-binding region. This higher resolution structure of CEACAM1 will facilitate a more precise dissection of its functional regions in the context of neisserial pathogenesis, cellular adhesion and immune evasion.
About this Structure
2GK2 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of human CEACAM1: binding target of the opacity proteins during invasion of Neisseria meningitidis and N. gonorrhoeae., Fedarovich A, Tomberg J, Nicholas RA, Davies C, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):971-9. Epub 2006, Aug 19. PMID:16929097
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