2h0b
From Proteopedia
(New page: 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=" | + | [[Image:2h0b.gif|left|200px]]<br /><applet load="2h0b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2h0b, resolution 2.100Å" /> | caption="2h0b, resolution 2.100Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Sheckler, L R.]] |
| - | [[Category: Sudhof, T | + | [[Category: Sudhof, T C.]] |
[[Category: Sugita, S.]] | [[Category: Sugita, S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: b-sandwich]] | [[Category: b-sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:53 2008'' |
Revision as of 15:36, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 17:36:53 2008
Categories: Bos taurus | Single protein | Henry, L. | Rudenko, G. | Sheckler, L R. | Sudhof, T C. | Sugita, S. | CA | GOL | B-sandwich
