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PDBsum entry 2bzx

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protein links
Sh3 domain PDB id
2bzx
Jmol
Contents
Protein chain
61 a.a. *
* Residue conservation analysis
PDB id:
2bzx
Name: Sh3 domain
Title: Atomic model of crkl-sh3c monomer
Structure: Crk-like protein. Chain: a. Fragment: sh3 domain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.80Å     R-factor:   0.317     R-free:   0.374
Authors: M.Harkiolaki,R.J.Gilbert,E.Y.Jones,S.M.Feller
Key ref:
M.Harkiolaki et al. (2006). The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal. Structure, 14, 1741-1753. PubMed id: 17161365 DOI: 10.1016/j.str.2006.09.013
Date:
24-Aug-05     Release date:   28-Sep-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P46109  (CRKL_HUMAN) -  Crk-like protein
Seq:
Struc:
303 a.a.
61 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.str.2006.09.013 Structure 14:1741-1753 (2006)
PubMed id: 17161365  
 
 
The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal.
M.Harkiolaki, R.J.Gilbert, E.Y.Jones, S.M.Feller.
 
  ABSTRACT  
 
CRKL plays essential roles in cell signaling. It consists of an N-terminal SH2 domain followed by two SH3 domains. SH2 and SH3N bind to signaling proteins, but the function of the SH3C domain has remained largely enigmatic. We show here that the SH3C of CRKL forms homodimers in protein crystals and in solution. Evidence for dimer formation of full-length CRKL is also presented. In the SH3C dimer, a nuclear export signal (NES) is mostly buried under the domain surface. The same is true for a monomeric SH3C obtained under different crystallization conditions. Interestingly, partial SH3 unfolding, such as occurs upon dimer/monomer transition, produces a fully-accessible NES through translocation of a single beta strand. Our results document the existence of an SH3 domain dimer formed through exchange of the first SH3 domain beta strand and suggest that partial unfolding of the SH3C is important for the relay of information in vivo.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. The CRKL SH3C Dimer
Schematic representation of the CRKL SH3C dimer (A), where the two polypeptide chains are colored green and red, respectively, with all β strands numbered from N to C terminus and a second view of the same structure (B) produced through a 90° clockwise rotation around the x axis of (A). The second orientation (B) is also viewed as a space-filling model (C). (D) C[α] models of the SH3C dimer and superimposed monomers. The two polypeptide chains in the dimer are colored green and red, respectively, while the monomers are in gray. The structures were superimposed in LSQKAB (Kabsch, 1976) with equivalences of core SH3 fold residues across species. Orientation same as in (A).
Figure 6.
Figure 6. Examples of Known SH3 Dimers
Ribbon representations of SH3 fold dimers (partner subunit polypeptide chains in green and red, respectively) of Vav and Grb2 (A) (Nishida et al., 2001), Grap2 (Mona/Gads) (B) (Harkiolaki et al., 2003), KorB-C (C), p47^phox (D) (Delbruck et al., 2002), and Eps8 (E) (Kishan et al., 1997). The yellow circle in (B) represents a crucial divalent metal ion.
 
  The above figures are reprinted by permission from Cell Press: Structure (2006, 14, 1741-1753) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21347241 P.C.Simister, F.Schaper, N.O'Reilly, S.McGowan, and S.M.Feller (2011).
Self-organization and regulation of intrinsically disordered proteins with folded N-termini.
  PLoS Biol, 9, e1000591.  
19307307 J.H.Seo, A.Suenaga, M.Hatakeyama, M.Taiji, and A.Imamoto (2009).
Structural and functional basis of a role for CRKL in a fibroblast growth factor 8-induced feed-forward loop.
  Mol Cell Biol, 29, 3076-3087.  
19426560 R.B.Birge, C.Kalodimos, F.Inagaki, and S.Tanaka (2009).
Crk and CrkL adaptor proteins: networks for physiological and pathological signaling.
  Cell Commun Signal, 7, 13.  
19861495 S.Antoku, and B.J.Mayer (2009).
Distinct roles for Crk adaptor isoforms in actin reorganization induced by extracellular signals.
  J Cell Sci, 122, 4228-4238.  
18697931 L.Wang, R.J.Gilbert, M.L.Atilano, S.R.Filipe, N.J.Gay, and P.Ligoxygakis (2008).
Peptidoglycan recognition protein-SD provides versatility of receptor formation in Drosophila immunity.
  Proc Natl Acad Sci U S A, 105, 11881-11886.  
18599349 N.Isakov (2008).
A new twist to adaptor proteins contributes to regulation of lymphocyte cell signaling.
  Trends Immunol, 29, 388-396.  
18200608 O.Okhrimenko, and I.Jelesarov (2008).
A survey of the year 2006 literature on applications of isothermal titration calorimetry.
  J Mol Recognit, 21, 1.  
18585411 W.Li, S.Yu, T.Liu, J.H.Kim, V.Blank, H.Li, and A.N.Kong (2008).
Heterodimerization with small Maf proteins enhances nuclear retention of Nrf2 via masking the NESzip motif.
  Biochim Biophys Acta, 1783, 1847-1856.  
17549081 D.Cowburn (2007).
Moving parts: how the adaptor protein CRK is regulated, and regulates.
  Nat Struct Mol Biol, 14, 465-466.  
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.