This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1zl8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zl8.gif|left|200px]]<br /><applet load="1zl8" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1zl8.gif|left|200px]]
-
caption="1zl8" />
+
 
-
'''NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins'''<br />
+
{{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==
Line 7: Line 16:
==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://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZL8 OCA].
+
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16147993 16147993]
+
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]]
Line 27: Line 36:
[[Category: specificity]]
[[Category: specificity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:40 2008''
+
''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


PDB ID 1zl8

Drag the structure with the mouse to rotate
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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools