The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer

Acta Crystallographica Section D: Biological Crystallography

Volumn 68, Issue 6, 2012, Pages 637-648

  Chen, Kai En ^a   Richards, Ayanthi A ^a   Ariffin, Juliana K ^a   Ross, Ian L ^a   Sweet, Matthew J ^a,b   Kellie, Stuart ^a,b   Kobe, Bostjan ^a,b   Martin, Jennifer L ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b The University of Queensland and QIMR Berghofer Medical Research Institute   (Australia)

Author keywords

domain swapping; DUF59; macrophages; protein protein interactions; zinc binding

Indexed keywords

CARRIER PROTEIN; CIAO1 PROTEIN, HUMAN; FAM96A PROTEIN, HUMAN; FAM96A PROTEIN, MOUSE; MESSENGER RNA; METALLOCHAPERONE;

ANIMAL; ARTICLE; C57BL MOUSE; CHEMICAL STRUCTURE; CHEMISTRY; HELA CELL; HUMAN; METABOLISM; MOUSE; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ANIMALS; CARRIER PROTEINS; CRYSTALLOGRAPHY, X-RAY; HELA CELLS; HUMANS; METALLOCHAPERONES; MICE; MICE, INBRED C57BL; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RNA, MESSENGER; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 84862233035     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444912006592     Document Type: Article

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