2h0b: Difference between revisions

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[[Image:2h0b.gif|left|200px]]
[[Image:2h0b.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_2h0b", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|GENE= NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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|DOMAIN=
{{STRUCTURE_2h0b| PDB=2h0b  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0b OCA], [http://www.ebi.ac.uk/pdbsum/2h0b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h0b RCSB]</span>
}}


'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha'''
'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha'''
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[[Category: Sudhof, T C.]]
[[Category: Sudhof, T C.]]
[[Category: Sugita, S.]]
[[Category: Sugita, S.]]
[[Category: b-sandwich]]
[[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 Mon Mar 31 03:23:39 2008''

Revision as of 02:43, 4 May 2008

File:2h0b.gif

Template:STRUCTURE 2h0b

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

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