2h0b: Difference between revisions
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'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha''' | {{Structure | ||
|PDB= 2h0b |SIZE=350|CAPTION= <scene name='initialview01'>2h0b</scene>, resolution 2.100Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |||
}} | |||
'''Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2H0B is a [ | 2H0B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0B OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16772286 16772286] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: b-sandwich]] | [[Category: b-sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:10:59 2008'' | ||
Revision as of 15:11, 20 March 2008
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| 2h0b, resolution 2.100Å | |||||||||||||
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| Ligands: | CA and GOL | ||||||||||||
| Gene: | NRXN1 (Bos taurus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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