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.


3biw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3biw.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3biw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3biw| PDB=3biw | SCENE= }}
{{STRUCTURE_3biw| PDB=3biw | SCENE= }}
-
'''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex'''
+
===Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex===
-
==Overview==
+
<!--
-
Neurexins and neuroligins provide trans-synaptic connectivity by the Ca2+-dependent interaction of their alternatively spliced extracellular domains. Neuroligins specify synapses in an activity-dependent manner, presumably by binding to neurexins. Here, we present the crystal structures of neuroligin-1 in isolation and in complex with neurexin-1 beta. Neuroligin-1 forms a constitutive dimer, and two neurexin-1 beta monomers bind to two identical surfaces on the opposite faces of the neuroligin-1 dimer to form a heterotetramer. The neuroligin-1/neurexin-1 beta complex exhibits a nanomolar affinity and includes a large binding interface that contains bound Ca2+. Alternatively spliced sites in neurexin-1 beta and in neuroligin-1 are positioned nearby the binding interface, explaining how they regulate the interaction. Structure-based mutations of neuroligin-1 at the interface disrupt binding to neurexin-1 beta, but not the folding of neuroligin-1 and confirm the validity of the binding interface of the neuroligin-1/neurexin-1 beta complex. Our results provide molecular insights for understanding the role of cell-adhesion proteins in synapse function.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18093522}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18093522 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18093522}}
==About this Structure==
==About this Structure==
Line 43: Line 47:
[[Category: Synapse]]
[[Category: Synapse]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:49:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:45:18 2008''

Revision as of 09:45, 29 July 2008

Image:3biw.png

Template:STRUCTURE 3biw

Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex

Template:ABSTRACT PUBMED 18093522

About this Structure

3BIW is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions., Arac D, Boucard AA, Ozkan E, Strop P, Newell E, Sudhof TC, Brunger AT, Neuron. 2007 Dec 20;56(6):992-1003. PMID:18093522

Page seeded by OCA on Tue Jul 29 12:45:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3biw"
Personal tools