1afo: Difference between revisions

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-[[Image:1afo.gif|left|200px]]
- {{Structure
+==DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES==
-|PDB= 1afo |SIZE=350|CAPTION= <scene name='initialview01'>1afo</scene>
+<StructureSection load='1afo' size='340' side='right'caption='[[1afo]]' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<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>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-|GENE=
+<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>
-}}
+</table>
+== Function ==
-'''DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES'''
+[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]]
-==Overview==
+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.
-==Disease==
+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>
-Known diseases associated with this structure: Blood group, MN OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=111300 111300]], Malaria, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=111300 111300]]
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-AFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFO OCA].
+</div>
+<div class="pdbe-citations 1afo" style="background-color:#fffaf0;"></div>
-==Reference==
+== References ==
-A transmembrane helix dimer: structure and implications., MacKenzie KR, Prestegard JH, Engelman DM, Science. 1997 Apr 4;276(5309):131-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9082985 9082985]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Engelman, D M.]]
+[[Category: Engelman DM]]
-[[Category: Mackenzie, K R.]]
+[[Category: Mackenzie KR]]
-[[Category: Prestegard, J H.]]
+[[Category: Prestegard JH]]
-[[Category: human glycophorin some]]
-[[Category: integral membrane protein]]
-[[Category: membrane protein folding]]
-[[Category: transmembrane helix interaction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:50 2008''