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4PLM

Crystal Structure of Chicken Netrin-1 (LN-LE3)

Summary for 4PLM
Entry DOI10.2210/pdb4plm/pdb
Related4PLN 4PLO
DescriptorNetrin-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
Functional Keywordselongated, cysteine rich, glycoprotein, protein binding
Biological sourceGallus gallus (Chicken)
Total number of polymer chains1
Total formula weight49344.61
Authors
Xu, K.,Nikolov, D.B. (deposition date: 2014-05-18, release date: 2014-06-18, Last modification date: 2024-10-16)
Primary citationXu, K.,Wu, Z.,Renier, N.,Antipenko, A.,Tzvetkova-Robev, D.,Xu, Y.,Minchenko, M.,Nardi-Dei, V.,Rajashankar, K.R.,Himanen, J.,Tessier-Lavigne, M.,Nikolov, D.B.
Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism.
Science, 344:1275-1279, 2014
Cited by
PubMed 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.
PubMed: 24876346
DOI: 10.1126/science.1255149
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.801 Å)
Structure validation

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