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PDBsum entry 5acm

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protein ligands Protein-protein interface(s) links
Immune system PDB id
5acm

 

 

 

 

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Contents
Protein chains
109 a.a.
Ligands
MBT
SO4 ×6
GOL
Waters ×208
PDB id:
5acm
Name: Immune system
Title: Mcg immunoglobulin variable domain with methylene blue
Structure: Mcg. Chain: a, b. Fragment: ig lambda chain v-ii region mgc. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.05Å     R-factor:   0.111     R-free:   0.122
Authors: B.Brumshtein,S.R.Esswein,L.Salwinski,M.L.Phillips,A.T.Ly,D.Cascio, M.R.Sawaya,D.S.Eisenberg
Key ref: B.Brumshtein et al. (2015). Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. Elife, 4, e10935. PubMed id: 26576950 DOI: 10.7554/eLife.10935
Date:
17-Aug-15     Release date:   02-Dec-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01709  (LV208_HUMAN) -  Immunoglobulin lambda variable 2-8 from Homo sapiens
Seq:
Struc:
118 a.a.
109 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 

 
DOI no: 10.7554/eLife.10935 Elife 4:e10935 (2015)
PubMed id: 26576950  
 
 
Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain.
B.Brumshtein, S.R.Esswein, L.Salwinski, M.L.Phillips, A.T.Ly, D.Cascio, M.R.Sawaya, D.S.Eisenberg.
 
  ABSTRACT  
 
Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can undergo irreversible aggregation to the amyloid state. The dimers therefore must disassociate into monomers prior to forming amyloid fibrils. Here we identify ligands that inhibit amyloid formation by stabilizing the Mcg light chain variable domain dimer and shifting the equilibrium away from the amyloid-prone monomer.
 

 

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