| 原文章发表时间:2010/12/3 |
| <标题>The dimer crystal structure explains8 ------------------------------------------------------ |
| <内容> The dimer crystal structure explains8 It was suggested using coimmunoprecipitation terminal blocks studies that the subtype specific heteromerization of cummins generator iGluRs is determined exclusively by the ATD in AMPA blind motor receptors5. However, it was shown later that besides glass bottle the ATD, compatibility of both the transmembrane table cloth domains and the C-terminal part of the ligand binding coach purses domain are also critical determinants for the formation of billig ugg functional channels6. A two step assembly of dimer-of-dimers was proposed moncler coat whereby the ATDs provide the initial signal for formation of dimers, and moncler jakker then tetrameric channels are formed by secondary ugg boot interactions involving the ligand binding and membrane ugg australia domains. The high affinity for dimer formation by the GluR6 ATD is consistent ugg aus with this proposal. More recently, functional studies based on chimeras shop moncler which exchanged ATD residues between GluR3 and GluR6 identified two sub- domains, N1 and N3 that are critical for subunit moncler winterjas assembly and which are key determinants jacket moncler of AMPA versus kainate subtype coassembly7. These ugg chimeras were designed based on homology models using the mGluR1 ugg bottes pas cher structure. When mapped to the GluR6 ATD dimer crystal structure bottes ugg pas cheres loop 1 is a part of the N1 subdomain while, loops 2 and 3 are ugg pas chers part of the N3 subdomain (Supplementary Fig. 5). This further collezione moncler emphasizes the role of these loops in controlling subtype specific iGluR giubbini moncler assembly. In contrast, swapping the N2 or N4 subdomains in moncler outlet GluR3 and GluR6 chimeras preserved functional heteromerization with wild type receptors indicating no role in the selective assembly of AMPA and kainate receptors. Our structure shows that N2 subdomain giubbini moncler corresponds to the R2 dimer interface where the interactions are primarily hydrophobic and relatively non piumino moncler specific, and for which the interacting residues are conserved moncler 2010 in non-NMDA receptors. In contrast, the N4 subdomain forms the giubbini moncler outer edge of each subunit and has no role in dimer formation. It is intriguing that in the domain piumino moncler R2 dimer surface for NMDA receptors alternative splicing of exon 5 in moncler coats the NR1 subunit controls polyamine and pH sensitivity. The cheap bridal gowns substitution of hydrophobic amino acids in the domain R2 formal wedding dresses surface of AMPA and kainate receptors by polar and charged residues in NMDA receptors creates potential binding sites buy rs accounts for polyamines at the dimer interface. |
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