2igh: Difference between revisions

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-{{Seed}}
-[[Image:2igh.png|left|200px]]
-<!--
+==DETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND III OF PROTEIN G FROM STREPTOCOCCUS BY 1H NMR==
-The line below this paragraph, containing "STRUCTURE_2igh", creates the "Structure Box" on the page.
+<StructureSection load='2igh' size='340' side='right'caption='[[2igh]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_2igh|  PDB=2igh  |  SCENE=  }}
+</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.
-===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 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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2igh" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_1474588}}, adds the Publication Abstract to the page
+*[[Protein G|Protein G]]
-(as it appears on PubMed at http://www.pubmed.gov), where 1474588 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_1474588}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-IGH is a [[Single protein]] structure of sequence from [http://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].
+[[Category: Streptococcus sp. GX7805]]
+[[Category: Derrick JP]]
-==Reference==
+[[Category: Lian L-Y]]
-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]
+[[Category: Roberts GCK]]
-[[Category: Single protein]]
+[[Category: Sutcliffe MJ]]
-[[Category: Streptococcus sp. gx7805]]
+[[Category: Yang JC]]
-[[Category: Derrick, J P.]]
-[[Category: Lian, L Y.]]
-[[Category: Roberts, G C.K.]]
-[[Category: Sutcliffe, M J.]]
-[[Category: Yang, J C.]]
-[[Category: Immunoglobulin-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:59:41 2008''