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Cytoplasmic terminus
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Membrane proteins define biological functions of membranes in cells. Extracellular peptides of transmembrane proteins receive signals from pathogens or environments, and are the major targets of drug developments.
8p
vihamax2711
21-04-2020
10
1
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The Arabidopsis FAE1 b-ketoacyl-CoA synthase (FAE1 KCS) catalyzes the condensation of malonyl-CoA with longchain acyl-CoAs. Sequence analysis of FAE1 KCS predicted that this condensing enzyme is anchored to a membrane by two adjacent N-terminal membrane-spanning domains. In order to characterize the FAE1 KCS and analyze its mechanism, FAE1 KCS and its mutants were engineered with a His6-tag at their N-terminus, and expressed in Saccharomyces cerevisiae. The membrane-bound enzyme was then solubilized and purified to near homogeneity on a metal affinity column.
9p
research12
01-06-2013
41
2
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DNA cytosine methyltransferaseMspI(M.MspI) must require a different type of interaction of protein with DNA from other bacterial DNA cytosine methyltransferases (m5C-MTases) to evoke the topoisomerase activity that it possesses in addition toDNA-methylation ability. Thismay require a different structural organization in the solution phase from the reported consensus structural arrangement for m5C-MTases.
7p
research12
29-04-2013
44
2
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ATP-sensitive K + channels are an octameric assembly of two proteins, a sulfonylurea receptor (SUR1)and an ion conducting subunit (Kir 6.0). We have examined the role of the C-terminus of SUR1 by expressing a series of truncation mutants together with Kir6.2 stably in HEK293 cells. Bio-chemical analyses using coimmunoprecipitation indicate that SUR1 deletionmutants andKir6.2 assemble and that a SUR1 deletion mutant binds glibenclamide with high affin-ity.
11p
tumor12
22-04-2013
41
3
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The interaction with phospholipid bilayers of two synthetic peptides with sequences corresponding to a segment next to the native N-terminus and an internal region of the E2 structural hepatitis G virus (HGV⁄GBV-C) protein [E2(7–26) and E2(279–298), respectively] has been characterized. Both peptides are water soluble but associate spontaneously with bilayers, showing higher affinity for anionic than zwitterionic membranes.
11p
awards
06-04-2013
35
2
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The tumor suppressor protein, p53, selectively binds to supercoiled (sc) DNA lacking the specific p53 consensus binding sequence (p53CON). Using p53 deletion mutants, we have previously shown that the p53 C-terminal DNA-binding site (CTDBS) is critical for this binding.
12p
awards
05-04-2013
40
4
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Phosphorylation at multiple sites within the N-terminus of p53 promotes its dissociation from hdm2/mdm2 and sti-mulates its transcriptional regulatory potential. The large phosphoinositide 3-kinase-like kinases ataxia telangiectasia mutated gene product and the ataxia telangectasia and RAD-3-related kinase promote phosphorylation of human p53at Ser15andSer20, andare required for theactivationof p53 following DNA damage.
9p
awards
05-04-2013
56
4
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The solution structure of a recombinant mutant [rSP-C (FFI)] of the human surfactant-associatedprotein C (hSP-C) in a mixture of chloroform andmethanol was determined by high-resolution NMR spectroscopy. rSP-C (FFI) contains a helix from Phe5 to theC-terminal Leu34 andis thus longer by two residues than the helix of porcine SP-C (pSP-C), which is reportedto start at Val7 in the same solvent. Two sets of resonances at the C-terminus of the peptide were observed, which are explained by low-order oligomerization, probably dimerization of rSP-C (FFI) in its a-helical form. ...
10p
dell39
03-04-2013
34
3
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Báo cáo khoa học: Hypoxia induces expression of a GPI-anchorless splice variant of the prion protein
The human prion protein (PrP) is a glycoprotein with a glycosylphosphat-idylinositol (GPI) anchor at its C-terminus. Here we report alternative splic-ing within exon 2 of the PrPgene (PRNP) in the human glioblastoma cell line T98G. The open reading frame of the alternatively spliced mRNA lacked the GPI anchor signal sequence and encoded a 230 amino acid polypeptide.
12p
galaxyss3
07-03-2013
35
3
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In the course of systematic identification of peptide signaling molecules combined with the expressed sequence tag database fromHydra, we have identified a novel neuropeptide family that consists of two members with FRamide at the C-terminus; FRamide-1 (IPTGTLIFRamide) and FR-amide-2 (APGSLLFRamide).
11p
media19
04-03-2013
32
1
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Human neuronal growth inhibitory factor (hGIF) is able to inhibit the out-growth of neurons. As compared with the amino acid sequences of metallo-thionein 1⁄2, hGIF contains two insertions: a Thr at position 5 and an acidic hexapeptide EAAEAE(55–60) close to the C-terminus. Moreover, all mammalian growth inhibitory factor sequences contain a conserved CPCP(6–9) motif.
12p
viettel02
22-02-2013
30
1
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Glutaminyl cyclases (QCs) catalyze the formation of pyroglutamate resi-dues at the N-terminus of several peptides and proteins from plants and animals. Recently, isoenzymes of mammalian QCs have been identified. In order to gain further insight into the biochemical characteristics of iso-QCs, the human and murine enzymes were expressed in the secretory pathway ofPichia pastoris.
15p
viettel02
20-02-2013
27
2
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A novel class of molecular chaperones co-ordinates the assembly and targeting of complex metalloproteins by binding to an amino-terminal peptide of the cognate substrate. We have previously shown that the NarJ chaperone interacts with the N-terminus of the NarG subunit coming from the nitrate reductase complex, NarGHI.
10p
mobifone23
21-01-2013
43
4
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The Zrt⁄Irt-like protein (ZIP) family of transporter proteins is involved in the uptake of essential metal elements in plants. Two homologous ZIP genes fromThlaspi japonicum, TjZNT1andTjZNT2, encode products that share high amino acid sequence similarity except at the N-terminus and the cytoplasmic loop between transmembrane domains III and IV, and that have been shown to be Zn 2+ and Mn 2+ transporters, respectively.
8p
mobifone23
08-01-2013
56
2
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CopA, a P-type ATPase transporter involved in copper detoxification in Bacillus subtilis, contains two soluble Atx1-like domains separated by a short linker at its N-terminus, an arrangement that occurs widely in copper transporters from both prokaryotes and eukaryotes. Both domains were previously found to bind Cu(I) with very high affinity.
14p
cosis54
08-12-2012
50
1
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