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PDBsum entry 3qs7

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protein ligands Protein-protein interface(s) links
Cytokine/signaling protein PDB id
3qs7
Jmol PyMol
Contents
Protein chains
135 a.a.
328 a.a.
168 a.a.
259 a.a.
Ligands
NAG ×7
PDB id:
3qs7
Name: Cytokine/signaling protein
Title: Crystal structure of a human flt3 ligand-receptor ternary co
Structure: Sl cytokine. Chain: a, b, c, d. Fragment: extracellular domain (unp residues 27-160). Synonym: flt3 ligand, fms-related tyrosine kinase 3 ligand, engineered: yes. Fl cytokine receptor. Chain: e, f, g, h. Fragment: extracellular domain (unp residues 27-436). Synonym: tyrosine-protein kinase receptor flt3, fms-like ty
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: flt3lg. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: flt3, stk1. Expressed in: homo sapiens. Expression_system_taxid: 9606.
Resolution:
4.30Å     R-factor:   0.261     R-free:   0.281
Authors: K.Verstraete,S.N.Savvides
Key ref: K.Verstraete et al. (2011). Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex. Blood, 118, 60-68. PubMed id: 21389326 DOI: 10.1182/blood-2011-01-329532
Date:
19-Feb-11     Release date:   16-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P49771  (FLT3L_HUMAN) -  Fms-related tyrosine kinase 3 ligand
Seq:
Struc:
235 a.a.
135 a.a.*
Protein chains
Pfam   ArchSchema ?
P36888  (FLT3_HUMAN) -  Receptor-type tyrosine-protein kinase FLT3
Seq:
Struc:
 
Seq:
Struc:
993 a.a.
328 a.a.
Protein chain
Pfam   ArchSchema ?
P36888  (FLT3_HUMAN) -  Receptor-type tyrosine-protein kinase FLT3
Seq:
Struc:
 
Seq:
Struc:
993 a.a.
168 a.a.
Protein chain
Pfam   ArchSchema ?
P36888  (FLT3_HUMAN) -  Receptor-type tyrosine-protein kinase FLT3
Seq:
Struc:
 
Seq:
Struc:
993 a.a.
259 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains E, F, G, H: E.C.2.7.10.1  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP
+
[protein]-L-tyrosine
Bound ligand (Het Group name = NAG)
matches with 47.62% similarity
= ADP
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     cell differentiation   2 terms 
  Biochemical function     cytokine activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1182/blood-2011-01-329532 Blood 118:60-68 (2011)
PubMed id: 21389326  
 
 
Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
K.Verstraete, G.Vandriessche, M.Januar, J.Elegheert, A.V.Shkumatov, A.Desfosses, K.Van Craenenbroeck, D.I.Svergun, I.Gutsche, B.Vergauwen, S.N.Savvides.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22902366 J.Elegheert, N.Bracke, P.Pouliot, I.Gutsche, A.V.Shkumatov, N.Tarbouriech, K.Verstraete, A.Bekaert, W.P.Burmeister, D.I.Svergun, B.N.Lambrecht, B.Vergauwen, and S.N.Savvides (2012).
Allosteric competitive inactivation of hematopoietic CSF-1 signaling by the viral decoy receptor BARF1.
  Nat Struct Mol Biol, 19, 938-947.
PDB codes: 3uez 3uf2 3uf5 4adf 4adq
23076159 K.Verstraete, and S.N.Savvides (2012).
Extracellular assembly and activation principles of oncogenic class III receptor tyrosine kinases.
  Nat Rev Cancer, 12, 753-766.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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