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1zl8
From Proteopedia
(New page: 200px<br /> <applet load="1zl8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zl8" /> '''NMR structure of L27 heterodimer from C. el...) |
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| - | [[Image:1zl8.gif|left|200px]]<br /> | + | [[Image:1zl8.gif|left|200px]]<br /><applet load="1zl8" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zl8" size=" | + | |
caption="1zl8" /> | caption="1zl8" /> | ||
'''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins'''<br /> | '''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins'''<br /> | ||
==Overview== | ==Overview== | ||
| - | LIN-2/7 (L27) domains are protein interaction modules that preferentially | + | 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== | ==About this Structure== | ||
| - | 1ZL8 is a [http://en.wikipedia.org/wiki/Protein_complex 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:// | + | 1ZL8 is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Dotsch, V.]] | [[Category: Dotsch, V.]] | ||
| - | [[Category: Lim, W | + | [[Category: Lim, W A.]] |
[[Category: Lohr, F.]] | [[Category: Lohr, F.]] | ||
| - | [[Category: Ou, H | + | [[Category: Ou, H D.]] |
| - | [[Category: Petrosky, K | + | [[Category: Petrosky, K Y.]] |
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
[[Category: assembly]] | [[Category: assembly]] | ||
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[[Category: specificity]] | [[Category: specificity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:40 2008'' |
Revision as of 14:16, 21 February 2008
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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 Feb 21 16:16:40 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
