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1y01

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Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin

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Retrieved from "http://52.214.119.220/wiki/index.php/1y01"

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-[[Image:1y01.gif|left|200px]]<br />
-<applet load="1y01" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1y01, resolution 2.8&Aring;" />
-'''Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin'''<br />
-==Overview==
+==Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin==
-Hemoglobin A (HbA), the oxygen delivery system in humans, comprises two, alpha and two beta subunits. Free alpha-hemoglobin (alphaHb) is unstable, and its precipitation contributes to the pathophysiology of beta, thalassemia. In erythrocytes, the alpha-hemoglobin stabilizing protein, (AHSP) binds alphaHb and inhibits its precipitation. The crystal structure, of AHSP bound to Fe(II)-alphaHb reveals that AHSP specifically recognizes, the G and H helices of alphaHb through a hydrophobic interface that, largely recapitulates the alpha1-beta1 interface of hemoglobin. The, AHSP-alphaHb interactions are extensive but suboptimal, explaining why, beta-hemoglobin can competitively displace AHSP to form HbA. Remarkably, the Fe(II)-heme group in AHSP bound alphaHb is coordinated by the distal, but not the proximal histidine. Importantly, binding to AHSP facilitates, the conversion of oxy-alphaHb to a deoxygenated, oxidized [Fe(III)], nonreactive form in which all six coordinate positions are occupied. These, observations reveal the molecular mechanisms by which AHSP stabilizes free, alphaHb.
+<StructureSection load='1y01' size='340' side='right'caption='[[1y01]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1y01]] is a 2 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=1Y01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y01 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHK:6-[(CYCLOHEXYLACETYL)(2-HYDROXYETHYL)AMINO]-6-DEOXY-D-XYLO-HEXITOL'>CHK</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1y01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y01 OCA], [https://pdbe.org/1y01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y01 RCSB], [https://www.ebi.ac.uk/pdbsum/1y01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y01 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== 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/y0/1y01_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=1y01 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-Y01 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM, OXY and CHK as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y01 OCA].
+*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
+== References ==
-==Reference==
+<references/>
-Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin., Feng L, Gell DA, Zhou S, Gu L, Kong Y, Li J, Hu M, Yan N, Lee C, Rich AM, Armstrong RS, Lay PA, Gow AJ, Weiss MJ, Mackay JP, Shi Y, Cell. 2004 Nov 24;119(5):629-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15550245 15550245]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Feng, L.]]
+[[Category: Feng L]]
-[[Category: Gell, D.A.]]
+[[Category: Gell DA]]
-[[Category: Gow, A.J.]]
+[[Category: Gow AJ]]
-[[Category: Gu, L.]]
+[[Category: Gu L]]
-[[Category: Mackay, J.P.]]
+[[Category: Mackay JP]]
-[[Category: Shi, Y.]]
+[[Category: Shi Y]]
-[[Category: Weiss, M.J.]]
+[[Category: Weiss MJ]]
-[[Category: Zhou, S.]]
+[[Category: Zhou S]]
-[[Category: CHK]]
-[[Category: HEM]]
-[[Category: OXY]]
-[[Category: ahsp]]
-[[Category: alpha hemoglobin]]
-[[Category: hemoglobin oxidation and precipitation]]
-[[Category: recognition]]
-[[Category: stabilization of alpha hemoglobin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:22:08 2007''

1y01

From Proteopedia

Current revision

Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin

Structural highlights

Function

Evolutionary Conservation

See Also

References

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