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PDBsum entry 5dn2

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protein ligands Protein-protein interface(s) links
Signaling protein PDB id
5dn2

 

 

 

 

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Contents
Protein chains
156 a.a.
Ligands
LYS-PRO-ARG-ARG ×2
CYS-ARG-CYS-ASP-
LYS-PRO-ARG-ARG
DIO ×2
GOL
Waters ×269
PDB id:
5dn2
Name: Signaling protein
Title: Human nrp2 b1 domain in complex with the peptide corresponding to the c-terminus of vegf-a
Structure: Neuropilin-2. Chain: a, b, c, d. Fragment: neuropilin-2 domain b1 f5/8 typE C 1, unp residues 275-429. Synonym: vascular endothelial cell growth factor 165 receptor 2. Engineered: yes. Vascular endothelial growth factor a. Chain: f, g, e. Fragment: vegf-a165-hbd, unp residues 205-232. Synonym: vegf-a,vascular permeability factor,vpf.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: nrp2, vegf165r2. Expressed in: escherichia coli. Expression_system_taxid: 83333. Expression_system_variant: rosetta-gami 2(de3)plyss. Gene: vegfa, vegf. Expression_system_variant: shuffle.
Resolution:
1.95Å     R-factor:   0.206     R-free:   0.234
Authors: Y.C.I.Tsai,P.Frankel,C.Fotinou,R.Rana,I.Zachary,S.Djordjevic
Key ref: Y.C.Tsai et al. (2016). Structural studies of neuropilin-2 reveal a zinc ion binding site remote from the vascular endothelial growth factor binding pocket. Febs J, 283, 1921-1934. PubMed id: 26991001 DOI: 10.1111/febs.13711
Date:
09-Sep-15     Release date:   20-Jul-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O60462  (NRP2_HUMAN) -  Neuropilin-2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
931 a.a.
156 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1111/febs.13711 Febs J 283:1921-1934 (2016)
PubMed id: 26991001  
 
 
Structural studies of neuropilin-2 reveal a zinc ion binding site remote from the vascular endothelial growth factor binding pocket.
Y.C.Tsai, C.Fotinou, R.Rana, T.Yelland, P.Frankel, I.Zachary, S.Djordjevic.
 
  ABSTRACT  
 
Neuropilin-2 is a transmembrane receptor involved in lymphangiogenesis and neuronal development. In adults, neuropilin-2 and its homologous protein neuropilin-1 have been implicated in cancers and infection. Molecular determinants of the ligand selectivity of neuropilins are poorly understood. We have identified and structurally characterized a zinc ion binding site on human neuropilin-2. The neuropilin-2-specific zinc ion binding site is located near the interface between domains b1 and b2 in the ectopic region of the protein, remote from the neuropilin binding site for its physiological ligand, i.e. vascular endothelial growth factor. We also present an X-ray crystal structure of the neuropilin-2 b1 domain in a complex with the C-terminal sub-domain of VEGF-A. Zn(2+) binding to neuropilin-2 destabilizes the protein structure but this effect was counteracted by heparin, suggesting that modifications by glycans and zinc in the extracellular matrix may affect functional neuropilin-2 ligand binding and signalling activity.
 

 

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