1zl8
From Proteopedia
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- | [[Image:1zl8.gif|left|200px]] | + | [[Image:1zl8.gif|left|200px]] |
- | + | ||
- | '''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins''' | + | {{Structure |
+ | |PDB= 1zl8 |SIZE=350|CAPTION= <scene name='initialview01'>1zl8</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |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]) | ||
+ | }} | ||
+ | |||
+ | '''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1ZL8 is a [ | + | 1ZL8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZL8 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16147993 16147993] |
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: specificity]] | [[Category: specificity]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:36:52 2008'' |
Revision as of 13:36, 20 March 2008
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Gene: | LIN7 (Caenorhabditis elegans), CASK, LIN2 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 15:36:52 2008
Categories: Caenorhabditis elegans | Homo sapiens | Protein complex | Dotsch, V. | Lim, W A. | Lohr, F. | Ou, H D. | Petrosky, K Y. | Alpha helix | Assembly | Heterodimer | L27 | Scaffold | Signaling | Specificity