The NMR structure of the recombinant human doppel protein, hDpl(24-152), contains a flexibly disordered "tail" comprising residues 24-51, and a globular domain extending from residues 52 to 149 for which a detailed structure was obtained. The globular domain contains four alpha-helices comprising residues 72-80 (alpha1), 101-115 (alpha2(a)), 117-121 (alpha2(b)), and 127-141 (alpha3), and a short two-stranded anti-parallel beta-sheet comprising residues 58-60 (beta1) and 88-90 (beta2). The fold of the hDpl globular domain thus coincides nearly identically with the structure of the murine Dpl protein. There are close similarities with the human prion protein (hPrP) but, similar to the situation with the corresponding murine proteins, hDpl shows marked local differences when compared to hPrP: the beta-sheet is flipped by 180 degrees with respect to the molecular scaffold formed by the four helices, and the beta1-strand is shifted by two residues toward the C terminus. A large solvent-accessible hydrophobic cleft is formed on the protein surface between beta2 and alpha3, which has no counterpart in hPrP. The helix alpha2 of hPrP is replaced by two shorter helices, alpha2(a) and alpha2(b). The helix alpha3 is shortened by more than two turns when compared with alpha3 of hPrP, which is enforced by the positioning of the second disulfide bond in hDpl. The C-terminal peptide segment 144-149 folds back onto the loop connecting beta2 and alpha2. All but four of the 20 conserved residues in the globular domains of hPrP and hDpl appear to have a structural role in maintaining a PrP-type fold. The conservation of R76, E96, N110 and R134 in hDpl, corresponding to R148, E168, N183 and R208 in hPrP suggests that these amino acid residues might have essential roles in the so far unknown functions of PrP and Dpl in healthy organisms.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
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Solution structure of the human Tax-interacting protein-1
Solution structure of the human Tax-interacting protein-1
Solution structure of the human Tax-interacting protein-1
Content Type Journal Article
Pages 329-334
DOI 10.1007/s10858-009-9361-8
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01-09-2011 12:46 PM
[NMR paper] NMR structure of human coactosin-like protein.
NMR structure of human coactosin-like protein.
Related Articles NMR structure of human coactosin-like protein.
J Biomol NMR. 2004 Nov;30(3):353-6
Authors: Liepinsh E, Rakonjac M, Boissonneault V, Provost P, Samuelsson B, Rådmark O, Otting G
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[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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[NMR paper] Influence of pH on NMR structure and stability of the human prion protein globular do
Influence of pH on NMR structure and stability of the human prion protein globular domain.
Related Articles Influence of pH on NMR structure and stability of the human prion protein globular domain.
J Biol Chem. 2003 Sep 12;278(37):35592-6
Authors: Calzolai L, Zahn R
The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and...
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[NMR paper] Prion protein NMR structure and familial human spongiform encephalopathies.
Prion protein NMR structure and familial human spongiform encephalopathies.
Related Articles Prion protein NMR structure and familial human spongiform encephalopathies.
Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11667-72
Authors: Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wüthrich K
The refined NMR structure of the mouse prion protein domain mPrP(121-231) and the recently reported NMR structure of the complete 208-residue polypeptide chain of mPrP are used to investigate the structural basis of inherited human transmissible...
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[NMR paper] Determination of the structure of the nucleocapsid protein NCp7 from the human immuno
Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR.
EMBO J. 1992 Aug;11(8):3059-65
Authors: Morellet N, Jullian N, De Rocquigny H, Maigret B, Darlix JL, Roques BP
The retroviral gag nucleocapsid protein NCp7 (72 amino acids)...
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[NMR paper] Protein secondary structure determination by NMR. Application with recombinant human
Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.
FEBS Lett. 1991 Jul 22;285(2):237-47
Authors: Wüthrich K, Spitzfaden C, Memmert K, Widmer H, Wider G
It is a unique trait of the NMR method for protein structure determination that a description of the polypeptide secondary...
NMR structure of the human doppel protein.
Linear Mode
