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1zl8
From Proteopedia
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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.]] | ||
| - | [[Category: | + | [[Category: Alpha helix]] |
| - | [[Category: | + | [[Category: Assembly]] |
| - | [[Category: | + | [[Category: Heterodimer]] |
| - | [[Category: | + | [[Category: L27]] |
| - | [[Category: | + | [[Category: Scaffold]] |
| - | [[Category: | + | [[Category: Signaling]] |
| - | [[Category: | + | [[Category: Specificity]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:45:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:45, 3 May 2008
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
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
