1afo: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1afo.png|left|200px]]
-<!--
+==DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES==
-The line below this paragraph, containing "STRUCTURE_1afo", creates the "Structure Box" on the page.
+<StructureSection load='1afo' size='340' side='right'caption='[[1afo]]' 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'>[[1afo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFO 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=1afo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afo OCA], [https://pdbe.org/1afo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afo RCSB], [https://www.ebi.ac.uk/pdbsum/1afo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afo ProSAT]</span></td></tr>
-{{STRUCTURE_1afo|  PDB=1afo  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GLPA_HUMAN GLPA_HUMAN] Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).<ref>PMID:8009226</ref> <ref>PMID:10926825</ref> <ref>PMID:12813056</ref> <ref>PMID:14604989</ref> <ref>PMID:15331714</ref> <ref>PMID:19438409</ref>
+== 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/af/1afo_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=1afo ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles. The GpA membrane-spanning alpha helices cross at an angle of -40 degrees and form a small but well-packed interface that lacks intermonomer hydrogen bonds. The structure provides an explanation for the previously characterized sequence dependence of GpA dimerization and demonstrates that van der Waals interactions alone can mediate stable and specific associations between transmembrane helices.
-===DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES===
+A transmembrane helix dimer: structure and implications.,MacKenzie KR, Prestegard JH, Engelman DM Science. 1997 Apr 4;276(5309):131-3. PMID:9082985<ref>PMID:9082985</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_9082985}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1afo" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9082985 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9082985}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[1afo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFO OCA].
-==Reference==
-<ref group="xtra">PMID:009082985</ref><ref group="xtra">PMID:009520409</ref><ref group="xtra">PMID:015208712</ref><ref group="xtra">PMID:018783247</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Engelman, D M.]]
+[[Category: Large Structures]]
-[[Category: Mackenzie, K R.]]
+[[Category: Engelman DM]]
-[[Category: Prestegard, J H.]]
+[[Category: Mackenzie KR]]
-[[Category: Human glycophorin some]]
+[[Category: Prestegard JH]]
-[[Category: Integral membrane protein]]
-[[Category: Membrane protein folding]]
-[[Category: Transmembrane helix interaction]]