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PDBsum entry 2ckn

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Transferase PDB id
2ckn

 

 

 

 

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Contents
Protein chain
95 a.a. *
* Residue conservation analysis
PDB id:
2ckn
Name: Transferase
Title: Nmr structure of the first ig module of mouse fgfr1
Structure: Basic fibroblast growth factor receptor 1. Chain: a. Fragment: ig1 module of mouse fgfr1, residues 25-119. Synonym: fgfr-1, bfgf-r, mfr. Engineered: yes
Source: Synthetic: yes. Mus musculus. Mouse. Organism_taxid: 10090
NMR struc: 20 models
Authors: V.V.Kiselyov,E.Bock,V.Berezin,F.M.Poulsen
Key ref:
V.V.Kiselyov et al. (2006). NMR structure of the first Ig module of mouse FGFR1. Protein Sci, 15, 1512-1515. PubMed id: 16731982 DOI: 10.1110/ps.062207906
Date:
20-Apr-06     Release date:   31-May-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16092  (FGFR1_MOUSE) -  Fibroblast growth factor receptor 1 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
822 a.a.
95 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.1  - receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
+ ATP
= O-phospho-L-tyrosyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1110/ps.062207906 Protein Sci 15:1512-1515 (2006)
PubMed id: 16731982  
 
 
NMR structure of the first Ig module of mouse FGFR1.
V.V.Kiselyov, E.Bock, V.Berezin, F.M.Poulsen.
 
  ABSTRACT  
 
Fibroblast growth factor (FGF) receptors (FGFRs) regulate a multitude of cellular processes during embryogenesis and in the adult. The extracellular part of the prototypical FGFR consists of three Ig modules (Ig1 - Ig3), in which Ig2 and Ig3 determine affinity and specificity for FGF and heparin, while the Ig1 module is thought to have a regulatory function. The crystal structures of the Ig2 and Ig3 modules alone and in complex with FGF have previously been reported. The structure of the Ig1 module is unknown, and very little is known about the structural determinants for the regulatory function of this module. We describe here the NMR structure of the Ig1 module of mouse FGFR1. The three-dimensional fold of the module belongs to the intermediate Ig subgroup and can be described as a beta-barrel consisting of two beta-sheets. One sheet is formed by A', G, F, C, and C', and the other by A, B, B', E, and D beta-strands. The overall strand topology of the Ig1 module is similar to that of the Ig2 and Ig3 modules. However, the A/A' loop of the Ig1 module is much longer than that of the Ig2 and Ig3 modules. It contains eight extra residues compared to the Ig3 module, and five extra residues compared to Ig2.
 
  Selected figure(s)  
 
Figure 1.
Structure of the FGFR1 Ig1 module. Stereo view of an overlay of the backbone atoms of 20 superimposed structures of the Ig1 module.
Figure 2.
Comparison of the secondary structures of the Ig1 and Ig3 modules of FGFR. (A) Ribbon representation of the structure of the Ig1 module. (B) Comparison of the structures of the A/A[prime prime or minute] loop region of the Ig1 and Ig3 modules.
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2006, 15, 1512-1515) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18593816 A.Kochoyan, F.M.Poulsen, V.Berezin, E.Bock, and V.V.Kiselyov (2008).
Structural basis for the activation of FGFR by NCAM.
  Protein Sci, 17, 1698-1705.  
17360555 B.M.Riley, M.A.Mansilla, J.Ma, S.Daack-Hirsch, B.S.Maher, L.M.Raffensperger, E.T.Russo, A.R.Vieira, C.Dodé, M.Mohammadi, M.L.Marazita, and J.C.Murray (2007).
Impaired FGF signaling contributes to cleft lip and palate.
  Proc Natl Acad Sci U S A, 104, 4512-4517.  
17008716 V.V.Kiselyov, A.Kochoyan, F.M.Poulsen, E.Bock, and V.Berezin (2006).
Elucidation of the mechanism of the regulatory function of the Ig1 module of the fibroblast growth factor receptor 1.
  Protein Sci, 15, 2318-2322.  
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.

 

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