Related Articles1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A.
Biochemistry. 1990 May 8;29(18):4466-78
Authors: Heald SL, Harding MW, Handschumacher RE, Armitage IM
Cyclophilin (163 residues, Mr 17737), a peptidyl prolyl cis-trans isomerase, is a cytosolic protein that specifically binds the potent immunosuppressant cyclosporin A (CsA). The native form of the major bovine thymus isoform has been analyzed by 2D NMR methods, COSY, HOHAHA, and NOESY, in aqueous media. The 156 main-chain amides in CyP yield 126 observable NH/alpha CH couplings (81%, Gly pairs counted as 1). Following exhaustive D2O exchange, 44 amide resonances remain visible. Further analysis of the NH/NH, NH/alpha CH, and alpha CH/alpha CH regions of the COSY and NOESY data sets indicates that the residual amides in D2O form a coherent hydrophobic domain which yields 2D NMR features suggestive of a beta-sheet. Many (43/126) of the amide resonances have been classified according to amino acid type. In the aromatic region of the spectra, the assignment of the ring spin systems is nearly complete (12/15 Phe, 2/2 Tyr, 1/1 Trp, and 3/4 His). This has successfully lead to the complete assignment of all of their beta CH's, main-chain alpha CH resonances, and many of the backbone amide resonances (8/12 Phe, 2/2 Tyr, 1/1 Trp, and 2/3 His). In other regions of the spectrum, the side-chain and main-chain resonances for 10/23 Gly, 9/9 Ala, 5/11 Thr, 5/9 Val, and 1/6 Leu have been completely assigned. The drug-free cyclophilin and CsA-bound cyclophilin form two discrete protein structures that are in slow exchange on the NMR time scale. Comparison of the fingerprint regions from the COSY spectra obtained from the two forms of the protein reveals a minimum of 16 cross-peaks which are clearly shifted upon complexation. In fact, on the basis of chemical shift changes observed in assigned side-chain and main-chain resonances, only a relatively few of the amino acid residues identified to date are perturbed by complex formation. These include 3 Phe (8, 12, and 14) and the Trp in the aromatic region and 2 Ala (7 and 8) in the Ala/Thr region. In the upfield-shifted methyl region, an assigned Leu and Val spin system and a spin system labeled X10 (an Ile or Leu) are affected by complex formation. In addition, a new aliphatic spin system, labeled X11, which shows a close spatial relationship to the perturbed Phe12, is observed in this region of the spectrum. In summary, the regions of the protein altered by complex formation can be divided into two categories: a hydrophobic and a H2O-accessible domain.(ABSTRACT TRUNCATED AT 400 WORDS)
[NMR paper] Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the e
Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
Related Articles Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
J Struct Biol. 2000 Aug;131(2):164-9
Authors: Hamdan S, Brown SE, Thompson PR, Yang JY, Carr PD, Ollis DL, Otting G, Dixon NE
The structured core of the N-terminal 3'-5' exonuclease domain of epsilon, the proofreading subunit of Escherichia coli DNA...
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[NMR paper] Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in
Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
FEBS Lett. 1997 Sep 29;415(2):155-9
Authors: Davydova NL, Rak AV, Gryaznova OI, Liljas A, Jonsson BH, Berglund H, Härd T, Garber MB
The gene for the ribosomal protein S19 from Thermus thermophilus was cloned,...
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[NMR paper] Cloning, purification, and preliminary characterization by circular dichroism and NMR
Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22...
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[NMR paper] Cloning, purification, and preliminary characterization by circular dichroism and NMR
Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22...
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[NMR paper] Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
Related Articles Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
J Chromatogr. 1991 Feb 22;539(2):501-5
Authors: Sweeney PJ, Walker JM, Reid DG, Elshourbagy N
Cloned trypanosomal calmodulin was expressed in Escherichia coli and purified to homogeneity using hydrophobic interaction chromatography on phenyl-Sepharose. The purified protein was subjected to NMR analysis which allows detailed changes to be observed when, firstly, calcium, and...
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[NMR paper] Sequence-specific 1H NMR assignments and structural characterization of bovine semina
Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Related Articles Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Biochemistry. 1991 Feb 12;30(6):1663-72
Authors: Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L, Llinás M
Sequence-specific resonance assignments for the isolated second or b domain of the bovine seminal fluid protein PDC-109 have been obtained from analysis of two-dimensional 1H...
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[NMR paper] 1H and 15N NMR resonance assignments and preliminary structural characterization of E
1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Related Articles 1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Biochemistry. 1991 Aug 6;30(31):7711-7
Authors: Feng YQ, Wand AJ, Sligar SG
The 1H and 15N resonances of uniformly enriched apocytochrome b562 (106 residues) have been assigned. The assignment work began with the identification of the majority of HN-H alpha-H beta subspin systems in...
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[NMR paper] 1H and 15N NMR resonance assignments and preliminary structural characterization of E
1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Related Articles 1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Biochemistry. 1991 Aug 6;30(31):7711-7
Authors: Feng YQ, Wand AJ, Sligar SG
The 1H and 15N resonances of uniformly enriched apocytochrome b562 (106 residues) have been assigned. The assignment work began with the identification of the majority of HN-H alpha-H beta subspin systems in...