1z8u

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[[Image:1z8u.gif|left|200px]]
 
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==Crystal structure of oxidized alpha hemoglobin bound to AHSP==
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The line below this paragraph, containing "STRUCTURE_1z8u", creates the "Structure Box" on the page.
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<StructureSection load='1z8u' size='340' side='right'caption='[[1z8u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1z8u]] is a 4 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=1Z8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z8U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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{{STRUCTURE_1z8u| PDB=1z8u | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z8u OCA], [https://pdbe.org/1z8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z8u RCSB], [https://www.ebi.ac.uk/pdbsum/1z8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z8u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AHSP_HUMAN AHSP_HUMAN] Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia.<ref>PMID:12066189</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z8/1z8u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1z8u ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of oxidized alpha hemoglobin bound to AHSP'''
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==See Also==
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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== References ==
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==Overview==
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<references/>
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The synthesis of haemoglobin A (HbA) is exquisitely coordinated during erythrocyte development to prevent damaging effects from individual alpha- and beta-subunits. The alpha-haemoglobin-stabilizing protein (AHSP) binds alpha-haemoglobin (alphaHb), inhibits the ability of alphaHb to generate reactive oxygen species and prevents its precipitation on exposure to oxidant stress. The structure of AHSP bound to ferrous alphaHb is thought to represent a transitional complex through which alphaHb is converted to a non-reactive, hexacoordinate ferric form. Here we report the crystal structure of this ferric alphaHb-AHSP complex at 2.4 A resolution. Our findings reveal a striking bis-histidyl configuration in which both the proximal and the distal histidines coordinate the haem iron atom. To attain this unusual conformation, segments of alphaHb undergo drastic structural rearrangements, including the repositioning of several alpha-helices. Moreover, conversion to the ferric bis-histidine configuration strongly and specifically inhibits redox chemistry catalysis and haem loss from alphaHb. The observed structural changes, which impair the chemical reactivity of haem iron, explain how AHSP stabilizes alphaHb and prevents its damaging effects in cells.
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Erythremias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Heinz body anemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Methemoglobinemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Thalassemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]]
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==About this Structure==
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1Z8U 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=1Z8U OCA].
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==Reference==
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Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem., Feng L, Zhou S, Gu L, Gell DA, Mackay JP, Weiss MJ, Gow AJ, Shi Y, Nature. 2005 Jun 2;435(7042):697-701. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15931225 15931225]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Feng, L.]]
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[[Category: Feng L]]
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[[Category: Gell, D A.]]
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[[Category: Gell DA]]
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[[Category: Gow, A J.]]
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[[Category: Gow AJ]]
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[[Category: Gu, L.]]
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[[Category: Gu L]]
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[[Category: Mackay, J P.]]
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[[Category: Mackay JP]]
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[[Category: Shi, Y.]]
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[[Category: Shi Y]]
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[[Category: Weiss, M J.]]
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[[Category: Weiss MJ]]
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[[Category: Zhou, S.]]
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[[Category: Zhou S]]
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[[Category: Ahsp]]
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[[Category: Alpha haemoglobin]]
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[[Category: Interaction]]
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[[Category: Oxidation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:19:24 2008''
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Current revision

Crystal structure of oxidized alpha hemoglobin bound to AHSP

PDB ID 1z8u

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