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991.
Mapping of POP1-binding site on pyrin domain of ASC 总被引:1,自引:0,他引:1
Srimathi T Robbins SL Dubas RL Chang H Cheng H Roder H Park YC 《The Journal of biological chemistry》2008,283(22):15390-15398
Apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) is an essential adaptor protein in the formation of a multiprotein complex that activates procaspase-1. ASC is also known as a modulator of NF-kappaB activation pathways. ASC has a bipartite domain structure, consisting of an N-terminal pyrin domain (PYD) and a C-terminal caspase-recruitment domain. The PYD of ASC (ASC_PYD) is known to interact with various PYD-containing intracellular danger signal sensors and PYD-only proteins. Using purified proteins, we characterized the in vitro interaction of ASC_PYD with PYD-only protein 1 (POP1). POP1 specifically interacts with ASC_PYD with a dissociation constant of 4.08 +/- 0.52 microm but does not interact with Cryopyrin. NMR and mutagenesis experiments show that a negative electrostatic potential surface patch (EPSP) on ASC_PYD, consisting of the first (H1) and fourth (H4) helices, is essential in the interaction with POP1. A positive EPSP on POP1, consisting of the second (H2) and third (H3) helices, is a counterpart of this interaction. The interaction between ASC_PYD and POP1 is similar to the interaction between caspase recruitment domains of Apaf-1 and procaspase-9. In addition, we present evidence that conformational changes at the long loop of ASC_PYD between the H2 and H3 helices can affect its interaction with POP1. Based on our observations, we propose that the positive EPSP of ASC_PYD, including the H2 and H3 helices, may be the binding site for Cryopyrin, and the interaction with Cryopyrin may induce the dissociation of POP1 from ASC_PYD. 相似文献
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Roelf Datema Rafael Pont Lezica Phillips W. Robbins Ralph T. Schwarz 《Archives of biochemistry and biophysics》1981,206(1):65-71
The UDP-derivative of deoxyglucose (UDP-deoxyglucose) inhibits the formation of dolichyl monophosphate glucose (Dol-P-glucose) in chick embryo cell membranes but has no effect on Dol-PP di-N-acetylchitobiose [Dol-PP-(GlcNAc)2]formation. The effects of UDP-deoxyglucose are not reversed by Dol-P, nor is Dol-P-deoxyglucose formed from this derivative. GDP-deoxyglucose inhibits formation of both Dol-P-glucose and Dol-PP-(GlcNAc)2. It is shown that GDP-deoxyglucose inhibits in these cases by competition with physiological nucleotide sugars for Dol-P. GDP-deoxyglucose and UDP-deoxyglucose also prevent the attachment of the peripheral glucose residues in Dol-PP-(GlcNAc)2-MansyGlc3, the immediate precursor of protein-bound oligosaccharides. The inhibition by GDP-deoxyglucose is only in part reversed by Dol-P, probably because deoxyglucose is incorporated into the lipid-linked oligosaccharide instead of glucose. 相似文献
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P P van Jaarsveld H Edelhoch D S Goodman J Robbins 《The Journal of biological chemistry》1973,248(13):4698-4705
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R C Robbins 《The Western journal of medicine》1975,122(5):421-422
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Quantification of myosin heavy-chain mRNA during myogenesis 总被引:4,自引:0,他引:4