1xzy

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[[Image:1xzy.jpg|left|200px]]
 
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{{Structure
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==Solution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)==
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|PDB= 1xzy |SIZE=350|CAPTION= <scene name='initialview01'>1xzy</scene>
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<StructureSection load='1xzy' size='340' side='right'caption='[[1xzy]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1xzy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XZY FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= AHSP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=1xzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xzy OCA], [https://pdbe.org/1xzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xzy RCSB], [https://www.ebi.ac.uk/pdbsum/1xzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xzy ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1w09|1W09]], [[1w0a|1W0A]], [[1w0b|1W0B]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xzy OCA], [http://www.ebi.ac.uk/pdbsum/1xzy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xzy RCSB]</span>
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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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}}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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'''Solution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)'''
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==Overview==
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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.
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.
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==About this Structure==
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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:15550245<ref>PMID:15550245</ref>
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1XZY is a [[Single protein]] structure of sequence 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=1XZY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://www.ncbi.nlm.nih.gov/pubmed/15550245 15550245]
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</div>
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<div class="pdbe-citations 1xzy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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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: Kong, Y.]]
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[[Category: Kong Y]]
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[[Category: Lee, C.]]
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[[Category: Lee C]]
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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: helical bundle]]
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[[Category: three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:57:00 2008''
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Current revision

Solution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)

PDB ID 1xzy

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