2h0b: Difference between revisions

New page: left|200px<br /><applet load="2h0b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h0b, resolution 2.100Å" /> '''Crystal Structure o...
 
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[[Image:2h0b.gif|left|200px]]<br /><applet load="2h0b" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2h0b.gif|left|200px]]<br /><applet load="2h0b" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2h0b, resolution 2.100&Aring;" />
caption="2h0b, resolution 2.100&Aring;" />
'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha'''<br />
'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha'''<br />


==Overview==
==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.
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==
==About this Structure==
2H0B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H0B OCA].  
2H0B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0B OCA].  


==Reference==
==Reference==
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[[Category: Henry, L.]]
[[Category: Henry, L.]]
[[Category: Rudenko, G.]]
[[Category: Rudenko, G.]]
[[Category: Sheckler, L.R.]]
[[Category: Sheckler, L R.]]
[[Category: Sudhof, T.C.]]
[[Category: Sudhof, T C.]]
[[Category: Sugita, S.]]
[[Category: Sugita, S.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: b-sandwich]]
[[Category: b-sandwich]]


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