2igh: Difference between revisions
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==DETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND III OF PROTEIN G FROM STREPTOCOCCUS BY 1H NMR== | ==DETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND III OF PROTEIN G FROM STREPTOCOCCUS BY 1H NMR== | ||
<StructureSection load='2igh' size='340' side='right' caption='[[2igh]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''> | <StructureSection load='2igh' size='340' side='right' caption='[[2igh]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2igh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_gx7809 Streptococcus gx7809]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IGH FirstGlance]. <br> | <table><tr><td colspan='2'>[[2igh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_gx7809 Streptococcus gx7809]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IGH FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2igh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igh OCA], [http://pdbe.org/2igh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2igh RCSB], [http://www.ebi.ac.uk/pdbsum/2igh PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2igh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igh OCA], [http://pdbe.org/2igh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2igh RCSB], [http://www.ebi.ac.uk/pdbsum/2igh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2igh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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/ig/2igh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ig/2igh_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> | ||
Revision as of 11:33, 4 July 2018
DETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND III OF PROTEIN G FROM STREPTOCOCCUS BY 1H NMRDETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND III OF PROTEIN G FROM STREPTOCOCCUS BY 1H NMR
Structural highlights
Function[SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. 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 PubMedWe have used 1H nuclear magnetic resonance spectroscopy to determine the solution structures of two small (61 and 64 residue) immunoglobulin G (IgG)-binding domains from protein G, a cell-surface protein from Streptococcus strain G148. The two domains differ in sequence by four amino acid substitutions, and differ in their affinity for some subclasses of IgG. The structure of domain II was determined using a total of 478 distance restraints, 31 phi and 9 chi 1 dihedral angle restraints; that of domain III was determined using a total of 445 distance restraints, 31 phi and 9 chi 1 dihedral angle restraints. A protocol which involved distance geometry, simulated annealing and restrained molecular dynamics was used to determine ensembles of 40 structures consistent with these restraints. The structures are found to consist of an alpha-helix packed against a four-stranded antiparallel-parallel-antiparallel beta-sheet. The structures of the two domains are compared to each other and to the reported structure of a similar domain from a protein G from a different strain of Streptococcus. We conclude that the difference in affinity of domains II and III for IgG is due to local changes in amino acid side-chains, rather than a more extensive change in conformation, suggesting that one or more of the residues which differ between them are directly involved in interaction with IgG. Determination of the solution structures of domains II and III of protein G from Streptococcus by 1H nuclear magnetic resonance.,Lian LY, Derrick JP, Sutcliffe MJ, Yang JC, Roberts GC J Mol Biol. 1992 Dec 20;228(4):1219-34. PMID:1474588[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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