PDBsum entry 4plm

Protein binding

PDB id: 4plm

Contents

Protein chain

416 a.a.

Ligands

NAG ×3

Metals

_MG

_CA

_CL ×2

Waters ×82

PDB id:

4plm

Name:

Protein binding

Title:

Crystal structure of chicken netrin-1 (ln-le3)

Structure:

Netrin-1. Chain: a. Fragment: ln-le3 (unp residues 26-457). Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Gene: ntn1. Expressed in: baculoviridae. Expression_system_taxid: 10442

Resolution:

2.80Å R-factor: 0.199 R-free: 0.257

Authors:

K.Xu,D.B.Nikolov

Key ref:

K.Xu et al. (2014). Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism. Science, 344, 1275-1279. PubMed id: 24876346 DOI: 10.1126/science.1255149

Date:

18-May-14 Release date: 18-Jun-14

Protein chain

Q90922  (NET1_CHICK) -  Netrin-1 from Gallus gallus

Seq: 606 a.a.

Struc: 416 a.a.

DOI no: 10.1126/science.1255149

Science 344:1275-1279 (2014)

PubMed id: 24876346

Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism.

K.Xu, Z.Wu, N.Renier, A.Antipenko, D.Tzvetkova-Robev, Y.Xu, M.Minchenko, V.Nardi-Dei, K.R.Rajashankar, J.Himanen, M.Tessier-Lavigne, D.B.Nikolov.

ABSTRACT

Netrins are secreted proteins that regulate axon guidance and neuronal migration. Deleted in colorectal cancer (DCC) is a well-established netrin-1 receptor mediating attractive responses. We provide evidence that its close relative neogenin is also a functional netrin-1 receptor that acts with DCC to mediate guidance in vivo. We determined the structures of a functional netrin-1 region, alone and in complexes with neogenin or DCC. Netrin-1 has a rigid elongated structure containing two receptor-binding sites at opposite ends through which it brings together receptor molecules. The ligand/receptor complexes reveal two distinct architectures: a 2:2 heterotetramer and a continuous ligand/receptor assembly. The differences result from different lengths of the linker connecting receptor domains fibronectin type III domain 4 (FN4) and FN5, which differs among DCC and neogenin splice variants, providing a basis for diverse signaling outcomes.