2aas: Difference between revisions
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==HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY== | ==HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY== | ||
<StructureSection load='2aas' size='340' side='right' caption='[[2aas]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''> | <StructureSection load='2aas' size='340' side='right'caption='[[2aas]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2aas]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AAS FirstGlance]. <br> | <table><tr><td colspan='2'>[[2aas]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AAS FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/2aas_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/2aas_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[RNase A NMR|RNase A NMR]] | *[[RNase A NMR|RNase A NMR]] | ||
*[[Ribonuclease|Ribonuclease]] | |||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bovin]] | [[Category: Bovin]] | ||
[[Category: Large Structures]] | |||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
[[Category: Bruix, M]] | [[Category: Bruix, M]] | ||
Revision as of 22:04, 11 December 2019
HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPYHIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Structural highlights
Function[RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHigh-resolution three-dimensional structures of bovine pancreatic ribonuclease A in aqueous solution have been determined by nuclear magnetic resonance (NMR) spectroscopy combined with restrained molecular dynamics calculations. The structures are based on: (1) 464 interproton distance constraints with accurate upper and lower limits, determined from build-up rates of nuclear Overhauser effects (NOE) by using the complete relaxation matrix; (2) 999 more approximate upper limits for interproton distances; and (3) 42 dihedral angle constraints (37 for phi and 5 for chi 1). A total of 16 structures were calculated, which show a root-mean-square (r.m.s.) deviation of 0.66 A for the backbone atoms and 1.68 A for all heavy-atoms. The converged structures are highly similar to those found in the crystal state. r.m.s. deviation of backbone atom positions in the crystal as compared to those in the average solution structure is 0.92 A. Observed differences are concentrated in loop regions and in the neighborhood of His119 and His48 side-chains. Dynamic aspects, such as H/D amide proton exchange and side-chain mobility have been examined. High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy.,Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J, Rico M J Mol Biol. 1993 Feb 5;229(3):722-34. PMID:8381876[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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