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PDBsum entry 1awx
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Transferase PDB id
1awx

 

 

 

 

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Contents
Protein chain
67 a.a. *
* Residue conservation analysis
PDB id:
1awx
Name: Transferase
Title: Sh3 domain from bruton's tyrosine kinase, nmr, minimized average structure
Structure: Bruton's tyrosine kinase. Chain: a. Fragment: sh3 domain. Synonym: atk, agmx1, bpk. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 1 models
Authors: H.Hansson,P.T.Mattsson,P.Allard,P.Haapaniemi,M.Vihinen,C.I.E.Smith, T.Hard
Key ref:
H.Hansson et al. (1998). Solution structure of the SH3 domain from Bruton's tyrosine kinase. Biochemistry, 37, 2912-2924. PubMed id: 9485443 DOI: 10.1021/bi972409f
Date:
06-Oct-97     Release date:   08-Apr-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q06187  (BTK_HUMAN) -  Tyrosine-protein kinase BTK from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		659 a.a.
67 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.2  - non-specific 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: 10.1021/bi972409f Biochemistry 37:2912-2924 (1998)
PubMed id: 9485443  
 
 
Solution structure of the SH3 domain from Bruton's tyrosine kinase.
H.Hansson, P.T.Mattsson, P.Allard, P.Haapaniemi, M.Vihinen, C.I.Smith, T.Hard.
 
  ABSTRACT  
 
X-linked agammaglobulinemia (XLA) is a heritable immunodeficiency caused by mutations in the gene coding for Bruton's tyrosine kinase (Btk). Btk belongs to the Tec family of tyrosine kinases. Each member of the family contains five regions and mutations causing XLA have been isolated in all five regions. We have determined the solution structure of the Src homology 3 (SH3) domain of Btk using two- and three-dimensional nuclear magnetic resonance (NMR) spectroscopy on natural abundance and 15N-labeled protein material. The structure determination is complemented by investigation of backbone dynamics based on 15N NMR relaxation. The Btk SH3 forms a well-defined structure and shows the typical SH3 topology of two short antiparallel beta-sheets packed almost perpendicular to each other in a sandwich-like fold. The N- and C-termini are more flexible as are peptide fragments in the RT and n-Src loops. The studied Btk SH3 fragment adopts two slowly interconverting conformations with a relative concentration ratio of 7:1. The overall fold of the minor form is similar to that of the major form, as judged on the basis of observed NOE connectivities and small chemical shift differences. A tryptophan (W251) ring flip is the favored mechanism for interconversion, although other possibilities cannot be excluded. The side chain of Y223, which becomes autophosphorylated upon activation of Btk, is exposed within the potential SH3 ligand binding site. Finally, we compare the present Btk SH3 structure with other SH3 structures.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19361414 A.Severin, R.E.Joseph, S.Boyken, D.B.Fulton, and A.H.Andreotti (2009).
Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain.
  J Mol Biol, 387, 726-743.  
19290922 R.E.Joseph, and A.H.Andreotti (2009).
Conformational snapshots of Tec kinases during signaling.
  Immunol Rev, 228, 74-92.  
18320328 A.Severin, D.B.Fulton, and A.H.Andreotti (2008).
Murine Itk SH3 domain.
  J Biomol NMR, 40, 285-290.  
17897671 R.E.Joseph, D.B.Fulton, and A.H.Andreotti (2007).
Mechanism and functional significance of Itk autophosphorylation.
  J Mol Biol, 373, 1281-1292.  
16969761 J.Väliaho, C.I.Smith, and M.Vihinen (2006).
BTKbase: the mutation database for X-linked agammaglobulinemia.
  Hum Mutat, 27, 1209-1217.  
16644721 L.Yu, A.J.Mohamed, L.Vargas, A.Berglöf, G.Finn, K.P.Lu, and C.I.Smith (2006).
Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1.
  J Biol Chem, 281, 18201-18207.  
15661031 J.M.Lindvall, K.E.Blomberg, J.Väliaho, L.Vargas, J.E.Heinonen, A.Berglöf, A.J.Mohamed, B.F.Nore, M.Vihinen, and C.I.Smith (2005).
Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling.
  Immunol Rev, 203, 200-215.  
15771581 L.J.Berg, L.D.Finkelstein, J.A.Lucas, and P.L.Schwartzberg (2005).
Tec family kinases in T lymphocyte development and function.
  Annu Rev Immunol, 23, 549-600.  
15044737 A.Mittermaier, and L.E.Kay (2004).
The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase.
  Protein Sci, 13, 1088-1099.  
12842872 H.M.Wilcox, and L.J.Berg (2003).
Itk phosphorylation sites are required for functional activity in primary T cells.
  J Biol Chem, 278, 37112-37121.  
12970174 J.A.Márquez, C.I.Smith, M.V.Petoukhov, P.Lo Surdo, P.T.Mattsson, M.Knekt, A.Westlund, K.Scheffzek, M.Saraste, and D.I.Svergun (2003).
Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.
  EMBO J, 22, 4616-4624.  
12717021 J.C.Ferreon, and V.J.Hilser (2003).
Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling.
  Protein Sci, 12, 982-996.  
12592021 R.Stoll, C.Renner, R.Buettner, W.Voelter, A.K.Bosserhoff, and T.A.Holak (2003).
Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
  Protein Sci, 12, 510-519.  
11742120 A.Laederach, K.W.Cradic, K.N.Brazin, J.Zamoon, D.B.Fulton, X.Y.Huang, and A.H.Andreotti (2002).
Competing modes of self-association in the regulatory domains of Bruton's tyrosine kinase: intramolecular contact versus asymmetric homodimerization.
  Protein Sci, 11, 36-45.  
11877742 M.P.Okoh, and M.Vihinen (2002).
Interaction between Btk TH and SH3 domain.
  Biopolymers, 63, 325-334.  
11340625 C.I.Smith, T.C.Islam, P.T.Mattsson, A.J.Mohamed, B.F.Nore, and M.Vihinen (2001).
The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk, Tec, Txk and homologs in other species.
  Bioessays, 23, 436-446.  
11316885 K.V.Kishan, M.E.Newcomer, T.H.Rhodes, and S.D.Guilliot (2001).
Effect of pH and salt bridges on structural assembly: molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain.
  Protein Sci, 10, 1046-1055.
PDB codes: 1i07 1i0c
  11206059 S.R.Tzeng, M.T.Pai, F.D.Lung, C.W.Wu, P.P.Roller, B.Lei, C.J.Wei, S.C.Tu, S.H.Chen, W.J.Soong, and J.W.Cheng (2000).
Stability and peptide binding specificity of Btk SH2 domain: molecular basis for X-linked agammaglobulinemia.
  Protein Sci, 9, 2377-2385.  
10220140 M.Vihinen, S.P.Kwan, T.Lester, H.D.Ochs, I.Resnick, J.Väliaho, M.E.Conley, and C.I.Smith (1999).
Mutations of the human BTK gene coding for bruton tyrosine kinase in X-linked agammaglobulinemia.
  Hum Mutat, 13, 280-285.  
9618763 C.I.Smith, C.M.Bäckesjö, A.Berglöf, L.J.Brandén, T.Islam, P.T.Mattsson, A.J.Mohamed, S.Müller, B.Nore, and M.Vihinen (1998).
X-linked agammaglobulinemia: lack of mature B lineage cells caused by mutations in the Btk kinase.
  Springer Semin Immunopathol, 19, 369-381.  
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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