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1QMC

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

Summary for 1QMC
Entry DOI10.2210/pdb1qmc/pdb
Related1A5V 1A5W 1A5X 1AUB 1B9D 1B9F 1BHL 1BI4 1BIS 1BIU 1BL3 1WJA 1WJB 1WJC 1WJD 1WJE 1WJF 2ITG
DescriptorHIV-1 INTEGRASE (1 entity in total)
Functional Keywordsintegrase, dna-binding protein, src homology 3 (sh3)-like fold, aids, polyprotein, transferase
Biological sourceHUMAN IMMUNODEFICIENCY VIRUS TYPE 1 BH10
Cellular locationGag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P03366
Total number of polymer chains2
Total formula weight12304.46
Authors
Eijkelenboom, A.P.A.M.,Sprangers, R.,Hard, K.,Puras Lutzke, R.A.,Plasterk, R.H.A.,Boelens, R.,Kaptein, R. (deposition date: 1999-09-27, release date: 1999-12-14, Last modification date: 2024-05-15)
Primary citationEijkelenboom, A.P.A.M.,Sprangers, R.,Hard, K.,Puras Lutzke, R.A.,Plasterk, R.H.A.,Boelens, R.,Kaptein, R.
Refined Solution Structure of the C-Terminal DNA-Binding Domain of Human Immunovirus-1 Integrase.
Proteins: Struct.,Funct., Genet., 36:556-, 1999
Cited by
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.
PubMed: 10450096
DOI: 10.1002/(SICI)1097-0134(19990901)36:4<556::AID-PROT18>3.3.CO;2-Y
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-11-06公开中

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