1c4r
From Proteopedia
(New page: 200px<br /><applet load="1c4r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c4r, resolution 2.60Å" /> '''THE STRUCTURE OF THE...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1c4r.gif|left|200px]]<br /><applet load="1c4r" size=" | + | [[Image:1c4r.gif|left|200px]]<br /><applet load="1c4r" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c4r, resolution 2.60Å" /> | caption="1c4r, resolution 2.60Å" /> | ||
'''THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING'''<br /> | '''THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Neurexins are expressed in hundreds of isoforms on the neuronal cell | + | 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== | ==About this Structure== | ||
| - | 1C4R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1C4R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4R OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Nguyen, T.]] | [[Category: Nguyen, T.]] | ||
[[Category: Rudenko, G.]] | [[Category: Rudenko, G.]] | ||
| - | [[Category: Sudhof, T | + | [[Category: Sudhof, T C.]] |
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: cell-cell adhesion]] | [[Category: cell-cell adhesion]] | ||
| Line 25: | Line 25: | ||
[[Category: neurobiology]] | [[Category: neurobiology]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:21 2008'' |
Revision as of 10:02, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 12:02:21 2008
