Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 7, 2014, Pages 2007-2018

  Eibl, Clarissa ^a,b   Hessenberger, Manuel ^a,c   Wenger, Julia ^a,d   Brandstetter, Hans ^a  

^a UNIVERSITY OF SALZBURG   (Austria)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^c MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^d UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

NLRP14; pyrin domain

Indexed keywords

CYTOSKELETON PROTEIN; MARENOSTRIN; NLRP14 PROTEIN, HUMAN; NUCLEOSIDE TRIPHOSPHATASE;

AMINO ACID SEQUENCE; CHEMISTRY; CIRCULAR DICHROISM; GEL CHROMATOGRAPHY; HUMAN; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CYTOSKELETAL PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEOSIDE-TRIPHOSPHATASE; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84904015766     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714010311     Document Type: Article

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