PDBsum entry: 1c4r

Membrane protein

PDB-id: 1c4r

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PROCHECK

Protein chains

180 a.a. *

Waters ×108

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

1c4r

Name:

Membrane protein

Title:

The structure of the ligand-binding domain of neurexin 1beta: regulation of lns domain function by alternative splicing

Structure:

Neurexin-i beta. Chain: a, b, c, d, e, f, g, h. Fragment: extracellular domain. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

UniProt:

Chains A, B, C, D, E, F, G, H: Q63373 (NRX1B_RAT)

Seq:

Struc:

Seq:

468 a.a.

Struc:

180 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

2.60Å

R-factor:

0.249

R-free:

0.279

Authors:

G.Rudenko,T.Nguyen,Y.Chelliah,T.C.Sudhof,J.Deisenhofer

Key ref:

G.Rudenko et al. (1999). The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing.. Cell, 99, 93. [PubMed id: 10520997] [DOI: 10.1016/S0092-8674(00)80065-3]

Date:

28-Sep-99

Release date:

04-Oct-00

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Key reference

DOI no: 10.1016/S0092-8674(00)80065-3

Cell 99:93 (1999)

PubMed id: 10520997

The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing.

G.Rudenko, T.Nguyen, Y.Chelliah, T.C.Südhof, J.Deisenhofer.

ABSTRACT

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.

Selected figure(s)

Figure 3.
Figure 3. Structural Similarity between Neurexin Iβ and Lectin DomainsThe neurexin Iβ structure (A) is compared to serum amyloid P protein (PDB ID code: 1sac [B]), glucanase (1axk [C]), and S-lectin (1slt [D]). A ribbon diagram (left) visualizes β strands in light blue or yellow and helices in magenta or green. Loops rising up over the concave surface forming part of the sugar binding pockets in 1sac, 1axk, and 1slt are shown in red, and their counterparts in neurexin Iβ are indicated as well. The molecular surfaces (right) are colored according to electrostatic potential with blue corresponding to +10 kT and red corresponding to −10 kT. Arrows indicate the carbohydrate-binding sites identified in the crystal structures.

Figure 5.
Figure 5. Alternative Splice SitesStereo C[α] trace of neurexin Iβ. Alternative splice sites identified in neurexin LNS domains are labeled #2, #3, #4, two sites identified in agrin LNS domains are labeled Y and Z. The equivalent position of the RGD sequence in human laminin A, implicated in integrin binding, is labeled with L.

The above figures are reprinted by permission from Cell Press: Cell (1999, 99, 93-0) copyright 1999.

Figures were selected by an automated process.