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2h0b

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(New page: 200px<br /><applet load="2h0b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h0b, resolution 2.100&Aring;" /> '''Crystal Structure o...)
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Revision as of 09:21, 21 November 2007

Image:2h0b.gif

2h0b, resolution 2.100Å

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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 with CA and GOL as ligands. 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

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