1QMC

C-terminal DNA-binding domain of HIV-1 integrase, NMR, 42 structures

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 42 
  • Selection Criteria: LOW OVERALL ENERGY 

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This is version 1.2 of the entry. See complete history. 


Literature

Refined Solution Structure of the C-Terminal DNA-Binding Domain of Human Immunovirus-1 Integrase.

Eijkelenboom, A.P.A.M., Sprangers, R., Hard, K., Puras Lutzke, R.A., Plasterk, R.H.A., Boelens, R., Kaptein, R.

(1999) Proteins 36: 556

  • DOI: https://doi.org/10.1002/(sici)1097-0134(19990901)36:4<556::aid-prot18>3.0.co;2-6
  • Primary Citation of Related Structures:  
    1QMC

  • PubMed Abstract: 

    The structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase has been refined using nuclear magnetic resonance spectroscopy. The protein is a dimer in solution and shows a well-defined dimer interface. The folding topology of the monomer consists of a five-stranded beta-barrel that resembles that of Src homology 3 domains. Compared with our previously reported structure, the structure is now defined far better. The final 42 structures display a back-bone root mean square deviation versus the average of 0.46 A. Correlation of the structure with recent mutagenesis studies suggests two possible models for DNA binding. Proteins 1999;36:556-564.

    • Organizational Affiliation: 

    Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HIV-1 INTEGRASE
A, B
52Human immunodeficiency virus type 1 BH10Mutation(s): 0 
UniProt
Find proteins for P03366 (Human immunodeficiency virus type 1 group M subtype B (isolate BH10))
Explore P03366 
Go to UniProtKB:  P03366
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03366
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 42 
  • Selection Criteria: LOW OVERALL ENERGY 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-12-14
    Type: Initial release
  • Version 1.1: 2015-10-14
    Changes: Database references, Derived calculations, Other, Source and taxonomy, Structure summary, Version format compliance
  • Version 1.2: 2024-05-15
    Changes: Data collection, Database references, Other