The dimeric structure of the Cpn60.2 chaperonin of Mycobacterium tuberculosis at 2.8 Å reveals possible modes of function

Journal of Molecular Biology

Volumn 412, Issue 2, 2011, Pages 192-203

  Shahar, Anat ^a   Melamed Frank, Meira ^a   Kashi, Yechezkel ^a   Shimon, Liat ^b   Adir, Noam ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

chaperone; heat shock proteins; protein interaction interfaces

Indexed keywords

CHAPERONIN; DIMER; PROTEIN CPN60.1; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; JOINT STIFFNESS; LIGHT SCATTERING; MACROPHAGE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLVATION;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS;

EID: 80052033133     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.026     Document Type: Article

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