1qz1

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[[Image:1qz1.jpg|left|200px]]
[[Image:1qz1.jpg|left|200px]]
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{{Structure
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|PDB= 1qz1 |SIZE=350|CAPTION= <scene name='initialview01'>1qz1</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1qz1", creates the "Structure Box" on the page.
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|SITE=
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|GENE= NCAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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{{STRUCTURE_1qz1| PDB=1qz1 | SCENE= }}
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|RELATEDENTRY=[[2ncm|2NCM]], [[3ncm|3NCM]], [[1epf|1EPF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qz1 OCA], [http://www.ebi.ac.uk/pdbsum/1qz1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qz1 RCSB]</span>
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'''Crystal Structure of the Ig 1-2-3 fragment of NCAM'''
'''Crystal Structure of the Ig 1-2-3 fragment of NCAM'''
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[[Category: Soroka, V.]]
[[Category: Soroka, V.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: ig module]]
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[[Category: Ig module]]
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[[Category: ncam]]
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[[Category: Ncam]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:52:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:06 2008''
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Revision as of 03:52, 3 May 2008

Image:1qz1.jpg

Template:STRUCTURE 1qz1

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 Page seeded by OCA on Sat May 3 06:52:35 2008

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