{"id":69,"date":"2017-09-26T03:25:28","date_gmt":"2017-09-26T01:25:28","guid":{"rendered":"http:\/\/www.bioactivescreeninglibrary.com\/?p=69"},"modified":"2022-01-07T10:42:59","modified_gmt":"2022-01-07T02:42:59","slug":"evolutionary-process-genes-encoding-disulphide-bondcontaining-proteins","status":"publish","type":"post","link":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/2017\/09\/26\/evolutionary-process-genes-encoding-disulphide-bondcontaining-proteins\/","title":{"rendered":"Evolutionary process of genes encoding disulphide bondcontaining proteins"},"content":{"rendered":"

In the view of the above results, we decided to study a TBCC truncation mutant containing the N-terminal domain FTY720<\/a> overexpressed in HeLa cells. In contrast to the cytoplasmic pattern observed for the full-length polypeptide, the TBCC N-terminal domain produced a dot-like pattern, distributed at the perinuclearcentrosomal region . As observed for the full-length construct, TBCC N-terminal domain overexpression was also associated with a number of metaphase aberrations . These results confirm a role for TBCC at the centrosome and support the hypothesis that the TBCC N-terminal domain is masked within this organelle. These data led us to study in more detail the TBCC N-terminal domain. Fig. 5A shows the superposition of the 20 conformers of the TBCC N-terminal domain determined by NMR. The structure is a left-handed 3-stranded a-helix bundle composed of 3 antiparallel and almost coaxial a-helices: a2, N56-R77; a3, V81-S101; a4, A107-L131 connected by short linkers: loop 2, A78-S80; loop 3, V102-A106. The N-terminal portion of this domain has not a defined orientation relative to the protein core and shows regions with partial helix formation . In particular, residues E33-K44 and N49-E55 adopt helical conformations with populations of ,60 and ,38%, respectively as estimated on the basis of their conformational shifts . No NOEs connect these nascent helices to the rest of the protein. The entire N-terminal region is structurally disordered relative to the domain and samples all the available conformational space. The structured part of the protein , is well-defined with low pairwise RMSD values . Average interhelical angles of 170u BU 4061T<\/a> between helix a2 and a3, 6u between helix a2 and a4, and 173u between helix a3 and a4 are obtained for the ensemble. The compact<\/a> helix bundle confers the molecule a rodlike shape with a volume of 11000 A \ufffd\ufffd 3 and a global accessible surface area of 6400 A \ufffd\ufffd 2 . Helical wheel projections show that the sequences of the three helices conforming the TBCC\ufffd\ufffds bundle fulfil the characteristic heptad pattern of lefthanded coiled coils . The side chains of a significant number of hydrophobic residues are deeply buried in the protein core, pointing to the interior of the helix bundle .<\/p>\n","protected":false},"excerpt":{"rendered":"

In the view of the above results, we decided to study a TBCC truncation mutant containing the N-terminal domain FTY720 overexpressed in HeLa cells. In contrast to the cytoplasmic pattern observed for the full-length polypeptide, the TBCC N-terminal domain produced a dot-like pattern, distributed at the perinuclearcentrosomal region . As observed for the full-length construct, … Continue reading “Evolutionary process of genes encoding disulphide bondcontaining proteins”<\/span><\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[1],"tags":[],"_links":{"self":[{"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/posts\/69"}],"collection":[{"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/comments?post=69"}],"version-history":[{"count":1,"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/posts\/69\/revisions"}],"predecessor-version":[{"id":70,"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/posts\/69\/revisions\/70"}],"wp:attachment":[{"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/media?parent=69"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/categories?post=69"},{"taxonomy":"post_tag","embeddable":true,"href":"http:\/\/www.bioactivescreeninglibrary.com\/index.php\/wp-json\/wp\/v2\/tags?post=69"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}