1c4r
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4r OCA], [http://www.ebi.ac.uk/pdbsum/1c4r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c4r RCSB]</span> | ||
}} | }} | ||
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[[Category: neurobiology]] | [[Category: neurobiology]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:14:29 2008'' |
Revision as of 16:14, 30 March 2008
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| , resolution 2.60Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING
Overview
Neurexins are expressed in hundreds of isoforms on the neuronal cell surface, where they may function as cell recognition molecules. Neurexins contain LNS domains, folding units found in many proteins like the G domain of laminin A, agrin, and slit. The crystal structure of neurexin Ibeta, a single LNS domain, reveals two seven-stranded beta sheets forming a jelly roll fold with unexpected structural similarity to lectins. The LNS domains of neurexin and agrin undergo alternative splicing that modulates their affinity for protein ligands in a neuron-specific manner. These splice sites are localized within loops at one edge of the jelly roll, suggesting a distinct protein interaction surface in LNS domains that is regulated by alternative splicing.
About this Structure
1C4R is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing., Rudenko G, Nguyen T, Chelliah Y, Sudhof TC, Deisenhofer J, Cell. 1999 Oct 1;99(1):93-101. PMID:10520997
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