3o81: Difference between revisions

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-'''Unreleased structure'''
-The entry 3o81 is ON HOLD  until Paper Publication
+==Beta2-microglobulin from Gallus gallus==
+<StructureSection load='3o81' size='340' side='right'caption='[[3o81]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3o81]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O81 FirstGlance]. <br>
+</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&#8491;</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=3o81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o81 OCA], [https://pdbe.org/3o81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o81 RCSB], [https://www.ebi.ac.uk/pdbsum/3o81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o81 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/B2MG_CHICK B2MG_CHICK] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+beta(2)-microglobulin (beta(2)m) is the smallest building block of molecules belonging to the immunoglobulin superfamily. By comparing thermodynamic and structural characteristics of chicken beta(2)m with those of other species, we seek to elucidate whether it is possible to pinpoint features that set the avian protein apart from other beta(2)m. The thermodynamic assays revealed that chicken beta(2)m exhibits a lower melting temperature than human beta(2)m, and the H/D exchange behavior observed by infrared spectroscopy indicates a more flexible structure of the former protein. To understand these differences at a molecular level, we determined the structure of free chicken beta(2)m by X-ray crystallography to a resolution of 2.0 A. Our comparisons indicate that certain biophysical characteristics of the chicken protein, particularly its conformational flexibility, diverge considerably from those of the other beta(2)m analyzed, although basic structural features have been retained through evolution.
-Authors: Loll, B., Hee, C.S., Uchanska-Ziegler, B., Ziegler, A.
+Comparative biophysical characterization of chicken beta2-microglobulin.,Hee CS, Fabian H, Uchanska-Ziegler B, Ziegler A, Loll B Biophys Chem. 2012 Jun;167:26-35. doi: 10.1016/j.bpc.2012.04.001. PMID:22695053<ref>PMID:22695053</ref>
-Description: Beta2-microglobulin from Gallus gallus
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3o81" style="background-color:#fffaf0;"></div>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:35:30 2010''
+==See Also==
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Hee CS]]
+[[Category: Loll B]]
+[[Category: Uchanska-Ziegler B]]
+[[Category: Ziegler A]]