Literature DB >> 22618865

¹H, ¹³C and ¹⁵N resonance assignments of the pyrin domain from human PYNOD.

Ming-Yuan Su1, Chung-I Chang, Chi-Fon Chang.   

Abstract

PYNOD is a novel protein belonging to a large family of proteins containing the nucleotide-binding and oligomerization domain (NOD) involved in inflammation and apoptosis. Human PYNOD inhibits inflammatory response mediated by caspase-1 and apoptosis-associated speck-like protein containing a caspase-recruitment domain (ASC). Here we report the (1)H, (13)C and (15)N resonance assignments and secondary structure identification of the pyrin domain (PYD) of human PYNOD as the first step towards elucidating the structural basis of the anti-inflammatory activity of PYNOD.

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Year:  2012        PMID: 22618865     DOI: 10.1007/s12104-012-9396-8

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  1 in total

1.  Three-dimensional structure of human NLRP10/PYNOD pyrin domain reveals a homotypic interaction site distinct from its mouse homologue.

Authors:  Ming-Yuan Su; Chiao-I Kuo; Chi-Fon Chang; Chung-I Chang
Journal:  PLoS One       Date:  2013-07-04       Impact factor: 3.240

  1 in total

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