2h0b: Difference between revisions

Revision as of 23:19, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2h0b.png

Template:STRUCTURE 2h0b

Crystal Structure of the second LNS/LG domain from Neurexin 1 alphaCrystal Structure of the second LNS/LG domain from Neurexin 1 alpha

Template:ABSTRACT PUBMED 16772286

About this StructureAbout this Structure

2H0B is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16772286}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16772286}}
 ==About this Structure==
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 [[Category: Sugita, S.]]
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