Related ArticlesThe X-ray structure of a recombinant major urinary protein at 1.75 A resolution. A comparative study of X-ray and NMR-derived structures.
Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1863-9
Authors: Kuser PR, Franzoni L, Ferrari E, Spisni A, Polikarpov I
Major urinary proteins belong to the lipocalin family and are present in the urine of rodents as an ensemble of isoforms with pheromonal activity. The crystal structure of a recombinant mouse MUP (rMUP) was solved by the molecular-replacement technique and refined to an R factor and R(free) of 20 and 26.5%, respectively, at 1.75 A resolution. The structure was compared with an NMR model and with a crystallographic structure of the wild-type form of the protein. The crystal structures determined in different space groups present significantly smaller conformational differences amongst themselves than in comparison with NMR models. Some, but not all, of the conformational differences between the crystal and solution structures can be explained by the influence of crystallographic contacts. Most of the differences between the NMR and X-ray structures were found in the N-terminus and loop regions. A number of side chains lining the hydrophobic pocket of the molecule are more tightly packed in the NMR structure than in the crystallographic model. Surprisingly, clear and continuous electron density for a ligand was observed inside the hydrophobic pocket of this recombinant protein. Conformation of the ligand modelled inside the density is coherent with the results of recent NMR experiments.
[NMR paper] NMR mapping of the recombinant mouse major urinary protein I binding site occupied by
NMR mapping of the recombinant mouse major urinary protein I binding site occupied by the pheromone 2-sec-butyl-4,5-dihydrothiazole.
Related Articles NMR mapping of the recombinant mouse major urinary protein I binding site occupied by the pheromone 2-sec-butyl-4,5-dihydrothiazole.
Biochemistry. 1999 Aug 3;38(31):9850-61
Authors: Zídek L, Stone MJ, Lato SM, Pagel MD, Miao Z, Ellington AD, Novotny MV
The interactions between the mouse major urinary protein isoform MUP-I and the pheromone 2-sec-butyl-4,5-dihydrothiazole have been characterized...
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[NMR paper] Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) f
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site.
Related Articles Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site.
Biochemistry. 1998 Aug 4;37(31):10881-96
Authors: Feng W, Tejero R, Zimmerman DE, Inouye M, Montelione GT
The major cold-shock protein (CspA) from Escherichia...
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[NMR paper] Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by sol
Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
Biochemistry. 1996 Apr 23;35(16):5145-57
Authors: Williams KA, Farrow NA, Deber CM, Kay LE
The structure and dynamics of the 53-residue filamentous bacteriophage IKe major coat protein in fully protonated myristoyllysophosphatidylglycerol (MPG)...
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[NMR paper] Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli:
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):5114-8
Authors: Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M, Montelione GT
Sequence-specific...
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[NMR paper] Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli:
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):5114-8
Authors: Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M, Montelione GT
Sequence-specific...
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[NMR paper] Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2
Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.
Related Articles Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.
J Biochem. 1993 Sep;114(3):421-31
Authors: Lancelin JM, Stein M, Jacquot JP
The recombinant form of the chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii that preferentially activates the NADP...
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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...
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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...