1ccz
From Proteopedia
(New page: 200px<br /> <applet load="1ccz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ccz, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ccz.gif|left|200px]]<br /> | + | [[Image:1ccz.gif|left|200px]]<br /><applet load="1ccz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ccz" size=" | + | |
caption="1ccz, resolution 1.8Å" /> | caption="1ccz, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CD2-BINDING DOMAIN OF CD58 (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3) AT 1.8-A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE CD2-BINDING DOMAIN OF CD58 (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3) AT 1.8-A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The binding of the cell surface molecule CD58 (formerly lymphocyte | + | The binding of the cell surface molecule CD58 (formerly lymphocyte function-associated antigen 3) to its ligand, CD2, significantly increases the sensitivity of antigen recognition by T cells. This was the first heterophilic cell adhesion interaction to be discovered and is now an important paradigm for analyzing the structural basis of cell-cell recognition. The crystal structure of a CD2-binding chimeric form of CD58, solved to 1.8-A resolution, reveals that the ligand binding domain of CD58 has the expected Ig superfamily V-set topology and shares several of the hitherto unique structural features of CD2, consistent with previous speculation that the genes encoding these molecules arose via duplication of a common precursor. Nevertheless, evidence for considerable divergence of CD2 and CD58 is also implicit in the structures. Mutations that disrupt CD2 binding map to the highly acidic surface of the AGFCC'C" beta-sheet of CD58, which, unexpectedly, lacks marked shape complementarity to the equivalent, rather more basic CD58-binding face of human CD2. The specificity of the very weak interactions of proteins mediating cell-cell recognition may often derive largely from electrostatic complementarity, with shape matching at the protein-protein interface being less exact than for interactions that combine specificity with high affinity, such as those involving antibodies. |
==About this Structure== | ==About this Structure== | ||
| - | 1CCZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CCZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Davis, S | + | [[Category: Davis, S J.]] |
[[Category: Harlos, K.]] | [[Category: Harlos, K.]] | ||
[[Category: Ikemizu, S.]] | [[Category: Ikemizu, S.]] | ||
| - | [[Category: Jones, E | + | [[Category: Jones, E Y.]] |
| - | [[Category: Merwe, P | + | [[Category: Merwe, P A.Van Der.]] |
| - | [[Category: Sparks, L | + | [[Category: Sparks, L M.]] |
| - | [[Category: Stuart, D | + | [[Category: Stuart, D I.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: cd58]] | [[Category: cd58]] | ||
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[[Category: lfa-3]] | [[Category: lfa-3]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:47 2008'' |
Revision as of 10:04, 21 February 2008
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CRYSTAL STRUCTURE OF THE CD2-BINDING DOMAIN OF CD58 (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3) AT 1.8-A RESOLUTION
Overview
The binding of the cell surface molecule CD58 (formerly lymphocyte function-associated antigen 3) to its ligand, CD2, significantly increases the sensitivity of antigen recognition by T cells. This was the first heterophilic cell adhesion interaction to be discovered and is now an important paradigm for analyzing the structural basis of cell-cell recognition. The crystal structure of a CD2-binding chimeric form of CD58, solved to 1.8-A resolution, reveals that the ligand binding domain of CD58 has the expected Ig superfamily V-set topology and shares several of the hitherto unique structural features of CD2, consistent with previous speculation that the genes encoding these molecules arose via duplication of a common precursor. Nevertheless, evidence for considerable divergence of CD2 and CD58 is also implicit in the structures. Mutations that disrupt CD2 binding map to the highly acidic surface of the AGFCC'C" beta-sheet of CD58, which, unexpectedly, lacks marked shape complementarity to the equivalent, rather more basic CD58-binding face of human CD2. The specificity of the very weak interactions of proteins mediating cell-cell recognition may often derive largely from electrostatic complementarity, with shape matching at the protein-protein interface being less exact than for interactions that combine specificity with high affinity, such as those involving antibodies.
About this Structure
1CCZ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution., Ikemizu S, Sparks LM, van der Merwe PA, Harlos K, Stuart DI, Jones EY, Davis SJ, Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4289-94. PMID:10200255
Page seeded by OCA on Thu Feb 21 12:04:47 2008
Categories: Homo sapiens | Single protein | Davis, S J. | Harlos, K. | Ikemizu, S. | Jones, E Y. | Merwe, P A.Van Der. | Sparks, L M. | Stuart, D I. | NAG | Cd58 | Crystal structure | Lfa-3
