1zl8

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[[Image:1zl8.gif|left|200px]]
[[Image:1zl8.gif|left|200px]]
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{{Structure
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|PDB= 1zl8 |SIZE=350|CAPTION= <scene name='initialview01'>1zl8</scene>
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The line below this paragraph, containing "STRUCTURE_1zl8", creates the "Structure Box" on the page.
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|GENE= LIN7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]), CASK, LIN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1zl8| PDB=1zl8 | SCENE= }}
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|RELATEDENTRY=[[1rso|1RSO]], [[1vf|1VF]], [[1y74|1Y74]], [[1y76|1Y76]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zl8 OCA], [http://www.ebi.ac.uk/pdbsum/1zl8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zl8 RCSB]</span>
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'''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins'''
'''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins'''
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[[Category: Ou, H D.]]
[[Category: Ou, H D.]]
[[Category: Petrosky, K Y.]]
[[Category: Petrosky, K Y.]]
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[[Category: alpha helix]]
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[[Category: Alpha helix]]
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[[Category: assembly]]
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[[Category: Assembly]]
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[[Category: heterodimer]]
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[[Category: Heterodimer]]
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[[Category: l27]]
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[[Category: L27]]
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[[Category: scaffold]]
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[[Category: Scaffold]]
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[[Category: signaling]]
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[[Category: Signaling]]
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[[Category: specificity]]
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[[Category: Specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:45:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:14 2008''
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Revision as of 14:45, 3 May 2008

Image:1zl8.gif

Template:STRUCTURE 1zl8

NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins


Overview

LIN-2/7 (L27) domains are protein interaction modules that preferentially hetero-oligomerize, a property critical for their function in directing specific assembly of supramolecular signaling complexes at synapses and other polarized cell-cell junctions. We have solved the solution structure of the heterodimer composed of the L27 domains from LIN-2 and LIN-7. Comparison of this structure with other L27 domain structures has allowed us to formulate a general model for why most L27 domains form an obligate heterodimer complex. L27 domains can be divided in two types (A and B), with each heterodimer comprising an A/B pair. We have identified two keystone positions that play a central role in discrimination. The residues at these positions are energetically acceptable in the context of an A/B heterodimer, but would lead to packing defects or electrostatic repulsion in the context of A/A and B/B homodimers. As predicted by the model, mutations of keystone residues stabilize normally strongly disfavored homodimers. Thus, L27 domains are specifically optimized to avoid homodimeric interactions.

About this Structure

1ZL8 is a Protein complex structure of sequences from Caenorhabditis elegans and Homo sapiens. Full crystallographic information is available from OCA.

Reference

A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes., Petrosky KY, Ou HD, Lohr F, Dotsch V, Lim WA, J Biol Chem. 2005 Nov 18;280(46):38528-36. Epub 2005 Sep 7. PMID:16147993 Page seeded by OCA on Sat May 3 17:45:51 2008

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