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1c4r

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THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING

Structural highlights

1c4r is a 8 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NRX1B_RAT Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nguyen T, Sudhof TC. Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules. J Biol Chem. 1997 Oct 10;272(41):26032-9. PMID:9325340
↑ Rudenko G, Nguyen T, Chelliah Y, Sudhof TC, Deisenhofer J. The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing. Cell. 1999 Oct 1;99(1):93-101. PMID:10520997

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c4r"

@@ Line 3: / Line 3: @@
 <StructureSection load='1c4r' size='340' side='right'caption='[[1c4r]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1c4r]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1c4r]] is a 8 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C4R FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1c4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c4r RCSB], [http://www.ebi.ac.uk/pdbsum/1c4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4r ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4r OCA], [https://pdbe.org/1c4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4r RCSB], [https://www.ebi.ac.uk/pdbsum/1c4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4r ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NRX1B_RAT NRX1B_RAT]] Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity).<ref>PMID:9325340</ref>
+[https://www.uniprot.org/uniprot/NRX1B_RAT NRX1B_RAT] Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity).<ref>PMID:9325340</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Chelliah, Y]]
+[[Category: Rattus norvegicus]]
-[[Category: Deisenhofer, J]]
+[[Category: Chelliah Y]]
-[[Category: Nguyen, T]]
+[[Category: Deisenhofer J]]
-[[Category: Rudenko, G]]
+[[Category: Nguyen T]]
-[[Category: Sudhof, T C]]
+[[Category: Rudenko G]]
-[[Category: Alternative splicing]]
+[[Category: Sudhof TC]]
-[[Category: Cell-cell adhesion]]
-[[Category: Cell-cell recognition]]
-[[Category: Lectin-like]]
-[[Category: Membrane protein]]
-[[Category: Neurobiology]]

1c4r

From Proteopedia

Current revision

THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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