1qz1
From Proteopedia
(New page: 200px<br /><applet load="1qz1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qz1, resolution 2.0Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1qz1.jpg|left|200px]]<br /><applet load="1qz1" size=" | + | [[Image:1qz1.jpg|left|200px]]<br /><applet load="1qz1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qz1, resolution 2.0Å" /> | caption="1qz1, resolution 2.0Å" /> | ||
'''Crystal Structure of the Ig 1-2-3 fragment of NCAM'''<br /> | '''Crystal Structure of the Ig 1-2-3 fragment of NCAM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent | + | The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent cell-cell and cell-substratum adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM molecules) binding. NCAM plays a key role in neural development, regeneration, and synaptic plasticity, including learning and memory consolidation. The crystal structure of a fragment comprising the three N-terminal Ig modules of rat NCAM has been determined to 2.0 A resolution. Based on crystallographic data and biological experiments we present a novel model for NCAM homophilic binding. The Ig1 and Ig2 modules mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), whereas the Ig3 module mediates interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through simultaneous binding to the Ig1 and Ig2 modules. This arrangement results in two perpendicular zippers forming a double zipper-like NCAM adhesion complex. |
==About this Structure== | ==About this Structure== | ||
| - | 1QZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1QZ1 is a [http://en.wikipedia.org/wiki/Single_protein 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=1QZ1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
[[Category: Kasper, C.]] | [[Category: Kasper, C.]] | ||
| - | [[Category: Kastrup, J | + | [[Category: Kastrup, J S.]] |
| - | [[Category: Kiselyov, V | + | [[Category: Kiselyov, V V.]] |
[[Category: Kolkova, K.]] | [[Category: Kolkova, K.]] | ||
| - | [[Category: Larsen, I | + | [[Category: Larsen, I K.]] |
| - | [[Category: Poulsen, F | + | [[Category: Poulsen, F M.]] |
[[Category: Soroka, V.]] | [[Category: Soroka, V.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
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[[Category: ncam]] | [[Category: ncam]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:14 2008'' |
Revision as of 12:45, 21 February 2008
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Crystal Structure of the Ig 1-2-3 fragment of NCAM
Overview
The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent cell-cell and cell-substratum adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM molecules) binding. NCAM plays a key role in neural development, regeneration, and synaptic plasticity, including learning and memory consolidation. The crystal structure of a fragment comprising the three N-terminal Ig modules of rat NCAM has been determined to 2.0 A resolution. Based on crystallographic data and biological experiments we present a novel model for NCAM homophilic binding. The Ig1 and Ig2 modules mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), whereas the Ig3 module mediates interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through simultaneous binding to the Ig1 and Ig2 modules. This arrangement results in two perpendicular zippers forming a double zipper-like NCAM adhesion complex.
About this Structure
1QZ1 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion., Soroka V, Kolkova K, Kastrup JS, Diederichs K, Breed J, Kiselyov VV, Poulsen FM, Larsen IK, Welte W, Berezin V, Bock E, Kasper C, Structure. 2003 Oct;11(10):1291-301. PMID:14527396
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