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PDBsum entry 4bqb

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protein ligands Protein-protein interface(s) links
Cell adhesion PDB id
4bqb

 

 

 

 

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Contents
Protein chains
195 a.a.
Ligands
NAG ×4
PDB id:
4bqb
Name: Cell adhesion
Title: Crystal structure of the fn5 and fn6 domains of neo1, form 2
Structure: Neogenin. Chain: a, b, c, d. Fragment: fn-type iii domains 5 and 6, residues 883-1133. Engineered: yes. Other_details: n-linked glycosylation at n940
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293t.
Resolution:
2.70Å     R-factor:   0.201     R-free:   0.223
Authors: C.H.Bell,E.Healey,S.Van Erp,B.Bishop,C.Tang,R.J.C.Gilbert, A.R.Aricescu,R.J.Pasterkamp,C.Siebold
Key ref: C.H.Bell et al. (2013). Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub. Science, 341, 77-80. PubMed id: 23744777 DOI: 10.1126/science.1232322
Date:
30-May-13     Release date:   12-Jun-13    
PROCHECK
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 Headers
 References

Protein chains
P97798  (NEO1_MOUSE) -  Neogenin from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1492 a.a.
195 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1126/science.1232322 Science 341:77-80 (2013)
PubMed id: 23744777  
 
 
Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub.
C.H.Bell, E.Healey, S.van Erp, B.Bishop, C.Tang, R.J.Gilbert, A.R.Aricescu, R.J.Pasterkamp, C.Siebold.
 
  ABSTRACT  
 
Repulsive guidance molecule family members (RGMs) control fundamental and diverse cellular processes, including motility and adhesion, immune cell regulation, and systemic iron metabolism. However, it is not known how RGMs initiate signaling through their common cell-surface receptor, neogenin (NEO1). Here, we present crystal structures of the NEO1 RGM-binding region and its complex with human RGMB (also called dragon). The RGMB structure reveals a previously unknown protein fold and a functionally important autocatalytic cleavage mechanism and provides a framework to explain numerous disease-linked mutations in RGMs. In the complex, two RGMB ectodomains conformationally stabilize the juxtamembrane regions of two NEO1 receptors in a pH-dependent manner. We demonstrate that all RGM-NEO1 complexes share this architecture, which therefore represents the core of multiple signaling pathways.
 

 

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