1iea: 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:1iea.gif|left|200px]]
- {{Structure
+==HISTOCOMPATIBILITY ANTIGEN==
-|PDB= 1iea |SIZE=350|CAPTION= <scene name='initialview01'>1iea</scene>, resolution 2.3&Aring;
+<StructureSection load='1iea' size='340' side='right'caption='[[1iea]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
+<table><tr><td colspan='2'>[[1iea]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEA FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1iea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iea OCA], [https://pdbe.org/1iea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iea RCSB], [https://www.ebi.ac.uk/pdbsum/1iea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iea ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HA21_MOUSE HA21_MOUSE]
+== 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/ie/1iea_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1iea ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The high-resolution x-ray crystal structures of the murine major histocompatibility complex (MHC) class II molecule, I-E(k), occupied by either of two antigenic peptides were determined. They reveal the structural basis for the I-E(k) peptide binding motif and suggest general principles for additional alleles. A buried cluster of acidic amino acids in the binding groove predicted to be conserved among all murine I-E and human DR MHC class II molecules suggests how pH may influence MHC binding or exchange of peptides. These structures also complement mutational studies on the importance of individual peptide residues to T cell receptor recognition.
-'''HISTOCOMPATIBILITY ANTIGEN'''
+Structures of an MHC class II molecule with covalently bound single peptides.,Fremont DH, Hendrickson WA, Marrack P, Kappler J Science. 1996 May 17;272(5264):1001-4. PMID:8638119<ref>PMID:8638119</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1iea" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The high-resolution x-ray crystal structures of the murine major histocompatibility complex (MHC) class II molecule, I-E(k), occupied by either of two antigenic peptides were determined. They reveal the structural basis for the I-E(k) peptide binding motif and suggest general principles for additional alleles. A buried cluster of acidic amino acids in the binding groove predicted to be conserved among all murine I-E and human DR MHC class II molecules suggests how pH may influence MHC binding or exchange of peptides. These structures also complement mutational studies on the importance of individual peptide residues to T cell receptor recognition.
+*[[MHC 3D structures|MHC 3D structures]]
+*[[MHC II 3D structures|MHC II 3D structures]]
-==About this Structure==
+== References ==
-IEA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEA OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-Structures of an MHC class II molecule with covalently bound single peptides., Fremont DH, Hendrickson WA, Marrack P, Kappler J, Science. 1996 May 17;272(5264):1001-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8638119 8638119]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Fremont DH]]
-[[Category: Fremont, D H.]]
+[[Category: Hendrickson WA]]
-[[Category: Hendrickson, W A.]]
+[[Category: Kappler J]]
-[[Category: Kappler, J.]]
+[[Category: Marrack P]]
-[[Category: Marrack, P.]]
-[[Category: NAG]]
-[[Category: histocompatibility antigen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:15 2008''