2LQN

Solution structure of CRKL


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 400 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII.

Jankowski, W.Saleh, T.Pai, M.T.Sriram, G.Birge, R.B.Kalodimos, C.G.

(2012) Nat Chem Biol 8: 590-596

  • DOI: https://doi.org/10.1038/nchembio.954
  • Primary Citation of Related Structures:  
    2LQN, 2LQW

  • PubMed Abstract: 

    CrkL is a key signaling protein that mediates the leukemogenic activity of Bcr-Abl. CrkL is thought to adopt a structure that is similar to that of its CrkII homolog. The two proteins share high sequence identity and indistinguishable ligand binding preferences, yet they have distinct physiological roles. Here we show that the structures of CrkL and phosphorylated CrkL are markedly different than the corresponding structures of CrkII. As a result, the binding activities of the Src homology 2 and Src homology 3 domains in the two proteins are regulated in a distinct manner and to a different extent. The different structural architecture of CrkL and CrkII may account for their distinct functional roles. The data show that CrkL forms a constitutive complex with Abl, thus explaining the strong preference of Bcr-Abl for CrkL. The results also highlight how the structural organization of the modular domains in adaptor proteins can control signaling outcome.


  • Organizational Affiliation

    Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Crk-like protein303Homo sapiensMutation(s): 0 
Gene Names: CRKL
UniProt & NIH Common Fund Data Resources
Find proteins for P46109 (Homo sapiens)
Explore P46109 
Go to UniProtKB:  P46109
PHAROS:  P46109
GTEx:  ENSG00000099942 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46109
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 400 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-05-16
    Type: Initial release
  • Version 1.1: 2012-06-06
    Changes: Database references
  • Version 1.2: 2015-10-14
    Changes: Other
  • Version 1.3: 2023-06-14
    Changes: Data collection, Database references, Other