2h0b
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2h0b.gif|left|200px]] | [[Image:2h0b.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2h0b", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_2h0b| PDB=2h0b | SCENE= }} | |
- | | | + | |
- | | | + | |
- | }} | + | |
'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha''' | '''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha''' | ||
Line 30: | Line 27: | ||
[[Category: Sudhof, T C.]] | [[Category: Sudhof, T C.]] | ||
[[Category: Sugita, S.]] | [[Category: Sugita, S.]] | ||
- | [[Category: | + | [[Category: B-sandwich]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:43:12 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 02:43, 4 May 2008
Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha
Overview
Neurexins mediate protein interactions at the synapse, playing an essential role in synaptic function. Extracellular domains of neurexins, and their fragments, bind a distinct profile of different proteins regulated by alternative splicing and Ca2+. The crystal structure of n1alpha_LNS#2 (the second LNS/LG domain of bovine neurexin 1alpha) reveals large structural differences compared with n1alpha_LNS#6 (or n1beta_LNS), the only other LNS/LG domain for which a structure has been determined. The differences overlap the so-called hyper-variable surface, the putative protein interaction surface that is reshaped as a result of alternative splicing. A Ca2+-binding site is revealed at the center of the hyper-variable surface next to splice insertion sites. Isothermal titration calorimetry indicates that the Ca2+-binding site in n1alpha_LNS#2 has low affinity (Kd approximately 400 microm). Ca2+ binding ceases to be measurable when an 8- or 15-residue splice insert is present at the splice site SS#2 indicating that alternative splicing can affect Ca2+-binding sites of neurexin LNS/LG domains. Our studies initiate a framework for the putative protein interaction sites of neurexin LNS/LG domains. This framework is essential to understand how incorporation of alternative splice inserts expands the information from a limited set of neurexin genes to produce a large array of synaptic adhesion molecules with potentially very different synaptic function.
About this Structure
2H0B is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the second LNS/LG domain from neurexin 1alpha: Ca2+ binding and the effects of alternative splicing., Sheckler LR, Henry L, Sugita S, Sudhof TC, Rudenko G, J Biol Chem. 2006 Aug 11;281(32):22896-905. Epub 2006 Jun 13. PMID:16772286 Page seeded by OCA on Sun May 4 05:43:12 2008