Related ArticlesNMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry. 1998 Sep 15;37(37):13021-32
Authors: Wang L, Yan H
The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M) has been determined by NMR spectroscopy. The sequential assignments of the 1H and 15N resonances of apo-R111M were established by multinuclear multidimensional NMR. The solution structure was calculated from 2302 distance restraints and 77 phi dihedral restraints derived from the NMR data. The root-mean-square deviation of the ensemble of 28 refined conformers that represent the structure from the mean coordinate set derived from them was 0.54 +/- 0.26 and 0.98 +/- 0.23 A for the backbone atoms and all heavy atoms, respectively. The solution structure of apo-R111M is similar to that of wild-type apo-CRABPII. However, there are significant conformational differences between the two proteins, localized mainly to three segments (Leu19-Ala36, Glu73-Cys81, and Leu99-Pro105) clustered around the ligand entrance more than 17 A away from the point mutation. In apo-R111M, all the three segments move toward the center of the ligand entrance so that the opening of the ligand-binding pocket in apo-R111M is much smaller than that in wild-type apo-CRABPII. Furthermore, the ligand-binding pocket of apo-R111M, especially the ligand entrance, is much less flexible than that of apo-CRABPII. Surprisingly, apo-R111M is more similar to holo-CRABPII than to apo-CRABPII in both structure and dynamical properties. The conformational and dynamical changes caused by the mutation are similar to those induced by binding of RA, although the magnitudes of the changes caused by the mutation are smaller than those induced by binding of RA. The results suggest that Arg111 plays a critical role in determining the structure and dynamical properties of CRABPII.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Biochim Biophys Acta. 2011 Aug 8;
Authors: Mertz B, Struts AV, Feller SE, Brown MF
Abstract
Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of...
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[NMR paper] NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitope
NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
Related Articles NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
J Biochem. 2005 Mar;137(3):255-63
Authors: Ichikawa S, Takai T, Inoue T, Yuuki T, Okumura Y, Ogura K, Inagaki F, Hatanaka H
Group 2 major mite allergens Der f 2 and Der p 2 are classified into...
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[NMR paper] NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
Related Articles NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
J Biol Chem. 2004 Sep 10;279(37):39035-41
Authors: Treviño MA, García-Mayoral MF, Barral P, Villalba M, Santoro J, Rico M, Rodríguez R, Bruix M
Ole e 6 is a pollen protein from the olive tree (Olea europaea) that exhibits allergenic activity with a high prevalence among olive-allergic individuals. The three-dimensional structure of Ole e 6 has been determined in solution by NMR...
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[NMR paper] The X-ray structure of a recombinant major urinary protein at 1.75 A resolution. A co
The X-ray structure of a recombinant major urinary protein at 1.75 A resolution. A comparative study of X-ray and NMR-derived structures.
Related Articles The 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...
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[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Related Articles The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat Struct Biol. 1998 May;5(5):393-9
Authors: Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding...
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[NMR paper] Expression and secondary structure determination by NMR methods of the major house du
Expression and secondary structure determination by NMR methods of the major house dust mite allergen Der p 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Expression and secondary structure determination by NMR methods of the major house dust mite allergen Der p 2.
J Biol Chem. 1997 Oct 24;272(43):26893-8
Authors: Mueller GA, Smith AM, Williams DC, Hakkaart GA, Aalberse RC, Chapman MD, Rule GS, Benjamin DC
There exists a strong...
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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] 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket st
1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Related Articles 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Biochemistry. 1991 Feb 19;30(7):1878-87
Authors: Lee KB, La Mar GN, Pandey RK, Rezzano IN, Mansfield KE, Smith KM
1H nuclear magnetic resonance spectroscopy was used to assign the hyperfine-shifted resonances and determine the position of...