1w72: Difference between revisions

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-{{Seed}}
-[[Image:1w72.png|left|200px]]
-<!--
+==Crystal structure of HLA-A1:MAGE-A1 in complex with Fab-Hyb3==
-The line below this paragraph, containing "STRUCTURE_1w72", creates the "Structure Box" on the page.
+<StructureSection load='1w72' size='340' side='right'caption='[[1w72]], [[Resolution|resolution]] 2.15&Aring;' 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'>[[1w72]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W72 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">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-{{STRUCTURE_1w72|  PDB=1w72  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w72 OCA], [https://pdbe.org/1w72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w72 RCSB], [https://www.ebi.ac.uk/pdbsum/1w72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w72 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref>   Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
+== 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/w7/1w72_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=1w72 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Antibodies with T cell receptor-like specificity possess a considerable diagnostic and therapeutic potential, but the structural basis of the interaction between an antibody and an histocompatibility antigen has so far not been determined. We present here the crystal structure (at 2.15 A resolution) of the recombinant, affinity-matured human antibody fragment Fab-Hyb3 bound to the tumor-associated human leukocyte antigen (HLA)/peptide complex HLA-A1.MAGE-A1. Fab-Hyb3 employs a diagonal docking mode resembling that of T cell receptors. However, other than these natural ligands, the antibody uses only four of its six complementarity-determining regions for direct interactions with the target. It recognizes the C-terminal half of the MAGE-A1 peptide, the HLA-A1 alpha1-helix, and N-terminal residues of the alpha2-helix, accompanied by a large tilting angle between the two types of molecules within the complex. Interestingly, only a single hydrogen bond between a peptide side chain and Fab-Hyb3 contributes to the interaction, but large buried surface areas with pronounced shape complementarity assure high affinity and specificity for MAGE-A1. The HLA-A1.MAGE-A1.antibody structure is discussed in comparison with those of natural ligands recognizing HLA.peptide complexes.
-===CRYSTAL STRUCTURE OF HLA-A1:MAGE-A1 IN COMPLEX WITH FAB-HYB3===
+A major histocompatibility complex-peptide-restricted antibody and t cell receptor molecules recognize their target by distinct binding modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1 in complex with FAB-HYB3.,Hulsmeyer M, Chames P, Hillig RC, Stanfield RL, Held G, Coulie PG, Alings C, Wille G, Saenger W, Uchanska-Ziegler B, Hoogenboom HR, Ziegler A J Biol Chem. 2005 Jan 28;280(4):2972-80. Epub 2004 Nov 10. PMID:15537658<ref>PMID:15537658</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1w72" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15537658}}, adds the Publication Abstract to the page
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15537658 is the PubMed ID number.
+*[[MHC 3D structures|MHC 3D structures]]
--->
+*[[MHC I 3D structures|MHC I 3D structures]]
-{{ABSTRACT_PUBMED_15537658}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-W72 is a [[Protein complex]] structure of sequences 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=1W72 OCA].
+</StructureSection>
-==Reference==
-A major histocompatibility complex-peptide-restricted antibody and t cell receptor molecules recognize their target by distinct binding modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1 in complex with FAB-HYB3., Hulsmeyer M, Chames P, Hillig RC, Stanfield RL, Held G, Coulie PG, Alings C, Wille G, Saenger W, Uchanska-Ziegler B, Hoogenboom HR, Ziegler A, J Biol Chem. 2005 Jan 28;280(4):2972-80. Epub 2004 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15537658 15537658]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Alings, C.]]
+[[Category: Alings C]]
-[[Category: Chames, P.]]
+[[Category: Chames P]]
-[[Category: Coulie, P G.]]
+[[Category: Coulie PG]]
-[[Category: Held, G.]]
+[[Category: Held G]]
-[[Category: Hillig, R C.]]
+[[Category: Hillig RC]]
-[[Category: Hoogenboom, H R.]]
+[[Category: Hoogenboom HR]]
-[[Category: Hulsmeyer, M.]]
+[[Category: Hulsmeyer M]]
-[[Category: Saenger, W.]]
+[[Category: Saenger W]]
-[[Category: Stanfield, R L.]]
+[[Category: Stanfield RL]]
-[[Category: Uchanska-Ziegler, B.]]
+[[Category: Uchanska-Ziegler B]]
-[[Category: Wille, G.]]
+[[Category: Wille G]]
-[[Category: Ziegler, A.]]
+[[Category: Ziegler A]]
-[[Category: Hla]]
-[[Category: Human leucocyte antigen]]
-[[Category: Mage]]
-[[Category: Mhc-i]]
-[[Category: Peptide-specific fab]]
-[[Category: Tcr-like binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:10:52 2008''