2igh: Difference between revisions

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-[[Image:2igh.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2igh", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2igh|  PDB=2igh  |  SCENE=  }}
-'''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]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2igh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._GX7805 Streptococcus sp. GX7805]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2IGH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2igh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igh OCA], [https://pdbe.org/2igh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igh RCSB], [https://www.ebi.ac.uk/pdbsum/2igh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2igh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We 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.
-==Overview==
+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<ref>PMID:1474588</ref>
-We 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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-IGH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._gx7805 Streptococcus sp. gx7805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGH OCA].
+</div>
+<div class="pdbe-citations 2igh" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/1474588 1474588]
+*[[Protein G|Protein G]]
-[[Category: Single protein]]
+== References ==
-[[Category: Streptococcus sp. gx7805]]
+<references/>
-[[Category: Derrick, J P.]]
+__TOC__
-[[Category: Lian, L Y.]]
+</StructureSection>
-[[Category: Roberts, G C.K.]]
+[[Category: Large Structures]]
-[[Category: Sutcliffe, M J.]]
+[[Category: Streptococcus sp. GX7805]]
-[[Category: Yang, J C.]]
+[[Category: Derrick JP]]
-[[Category: Immunoglobulin-binding protein]]
+[[Category: Lian L-Y]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:28:29 2008''
+[[Category: Roberts GCK]]
+[[Category: Sutcliffe MJ]]
+[[Category: Yang JC]]