1IN1

NMR STRUCTURE OF HUMAN DNA LIGASE IIIALPHA BRCT DOMAIN


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 299 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations, target function 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Solution structure and backbone dynamics of the human DNA ligase IIIalpha BRCT domain

Krishnan, V.V.Thornton, K.H.Thelen, M.P.Cosman, M.

(2001) Biochemistry 40: 13158-13166

  • DOI: https://doi.org/10.1021/bi010979g
  • Primary Citation of Related Structures:  
    1IMO, 1IN1

  • PubMed Abstract: 

    BRCT (BRCA1 carboxyl terminus) domains are found in a number of DNA repair enzymes and cell cycle regulators and are believed to mediate important protein-protein interactions. The DNA ligase IIIalpha BRCT domain partners with the distal BRCT domain of the DNA repair protein XRCC1 (X1BRCTb) in the DNA base excision repair (BER) pathway. To elucidate the mechanisms by which these two domains can interact, we have determined the solution structure of human ligase IIIalpha BRCT (L3[86], residues 837-922). The structure of L3[86] consists of a beta2beta1beta3beta4 parallel sheet with a two-alpha-helix bundle packed against one face of the sheet. This fold is conserved in several proteins having a wide range of activities, including X1BRCTb [Zhang, X. D., et al. (1998) EMBO J. 17, 6404-6411]. L3[86] exists as a dimer in solution, but an insufficient number of NOE restraints precluded the determination of the homodimer structure. However, 13C isotope-filtered and hydrogen-deuterium exchange experiments indicate that the N-terminus, alpha1, the alpha1-beta2 loop, and the three residues following alpha2 are involved in forming the dimer interface, as similarly observed in the structure of X1BRCTb. NOE and dynamic data indicate that several residues (837-844) in the N-terminal region appear to interconvert between helix and random coil conformations. Further studies of other BRCT domains and of their complexes are needed to address how these proteins interact with one another, and to shed light on how mutations can lead to disruption of function and ultimately disease.


  • Organizational Affiliation

    Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, Livermore, California 94551, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA LIGASE III88Homo sapiensMutation(s): 0 
EC: 6.5.1.1
UniProt & NIH Common Fund Data Resources
Find proteins for P49916 (Homo sapiens)
Explore P49916 
Go to UniProtKB:  P49916
PHAROS:  P49916
GTEx:  ENSG00000005156 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP49916
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 299 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations, target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-05-25
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-05-22
    Changes: Data collection