Related ArticlesSecondary structure of a complement control protein module by two-dimensional 1H NMR.
Biochemistry. 1991 Jan 29;30(4):997-1004
Authors: Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID
The complement control protein (CCP) module (also known as the short consensus repeat) is a consensus sequence of about 60 amino acid residues which is thought to fold independently. It occurs over 140 times in more than 20 extracellular mosaic proteins including 12 proteins of the complement cascade. An isolated CCP module, the 16th repeat from human complement factor H, has been expressed in a yeast vector and shown to fold with the same pattern of disulfide bond formation as is seen in the native protein. Two-dimensional 600-MHz 1H NMR spectra of this module have been recorded at pH 3.3 and 6.0 and analyzed to permit determination of secondary structure in solution. The CCP module comprises two predominantly extended segments (Glu1-His13 and Ala17-Glu27), two segments of double-stranded antiparallel beta-sheet (Gly14-Val16 paired with Tyr31-Cys33 and Gly38-Asp40 paired with Ser57-Ile59), and a short piece of triple-stranded beta-sheet (Glu27-Thr30, Ile44-Leu48, and Lys51-Ser53). Turns occur at Asp22, Gly36, and Glu50, while Gly41-Ala43 appear to form a looped-out segment or bulge. This structure is compared with a secondary structure prediction made on the basis of an alignment scheme of 101 sequences for CCP modules [Perkins, S. J., Haris, P. I., Sim, R. B., & Chapman, D. (1988) Biochemistry 27, 4004-4012]--the experimentally determined secondary structure bears an overall resemblance to the predicted one but differs in the number and position of turns. Some of those amino acid residues which are highly conserved throughout the range of CCP modules appear to play a role in stabilizing the global fold.
[NMR paper] NMR solution structure of complement-like repeat CR3 from the low density lipoprotein
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Feb 4;275(5):3264-9
Authors: Dolmer K, Huang W, Gettins PG
We have used NMR methods to determine the...
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[NMR paper] NMR studies of a viral protein that mimics the regulators of complement activation.
NMR studies of a viral protein that mimics the regulators of complement activation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of a viral protein that mimics the regulators of complement activation.
J Mol Biol. 1997 Sep 19;272(2):253-65
Authors: Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN
Vaccinia virus complement control protein (VCP) is a 243-residue protein that is similar in sequence to the regulators of complement activation; its...
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[NMR paper] The secondary structure of phospholamban: a two-dimensional NMR study.
The secondary structure of phospholamban: a two-dimensional NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The secondary structure of phospholamban: a two-dimensional NMR study.
Biochem Biophys Res Commun. 1995 Dec 26;217(3):1200-7
Authors: Maslennikov IV, Sobol AG, Anagli J, James P, Vorherr T, Arseniev AS, Carafoli E
Phospholamban (PLN) is an intrinsic membrane protein of 52 amino acids which regulates the Ca2+ pump of the sarcoplasmic reticulum of heart,...
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[NMR paper] Secondary structure of myristoylated recoverin determined by three-dimensional hetero
Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
Related Articles Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
Biochemistry. 1994 Sep 6;33(35):10743-53
Authors: Ames JB, Tanaka T, Stryer L, Ikura M
Recoverin, a new member of the EF-hand superfamily, serves as a Ca2+ sensor in vision. A myristoyl or related N-acyl group is covalently attached at its...
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[NMR paper] NMR determination of the secondary structure and the three-dimensional polypeptide ba
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
FEBS Lett. 1993 Nov 29;335(1):18-26
Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K
Nuclear magnetic resonance (NMR)...
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[NMR paper] 1H NMR assignment and secondary structure of the cell adhesion type III module of fib
1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin.
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Biochemistry. 1992 Feb 25;31(7):2068-73
Authors: Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID
The secondary structure of the tenth type III module from human fibronectin has been determined using NMR. This type of module appears many times in a wide variety of proteins. The type III module described here contains an...
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[NMR paper] Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution
Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
Eur J Biochem. 1990 Nov 13;193(3):789-99
Authors: Yu C, Lee CS, Chuang LC, Shei YR, Wang CY
The 1H-NMR spectra of cobrotoxin, a neurotoxic protein isolated from Formosan cobra Naja naja atra, have been studied by...
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[NMR paper] NMR solution structure of complement-like repeat CR8 from the low density lipoprotein
NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
J Biol Chem. 1999 May 14;274(20):14130-6
Authors: Huang W, Dolmer K, Gettins PG
The low density lipoprotein receptor-related protein is a member of the low density...