1y01: Difference between revisions

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{{Seed}}
[[Image:1y01.png|left|200px]]


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==Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin==
The line below this paragraph, containing "STRUCTURE_1y01", creates the "Structure Box" on the page.
<StructureSection load='1y01' size='340' side='right'caption='[[1y01]], [[Resolution|resolution]] 2.80&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'>[[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>
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]] 2.8&#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=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>
{{STRUCTURE_1y01|  PDB=1y01  |  SCENE=  }}
<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/initialview03.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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1y01" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15550245}}, adds the Publication Abstract to the page
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15550245 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_15550245}}
__TOC__
 
</StructureSection>
==Disease==
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]]
 
==About this Structure==
1Y01 is a 2 chains 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=1Y01 OCA].
 
==Reference==
<ref group="xtra">PMID:15550245</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Feng, L.]]
[[Category: Large Structures]]
[[Category: Gell, D A.]]
[[Category: Feng L]]
[[Category: Gow, A J.]]
[[Category: Gell DA]]
[[Category: Gu, L.]]
[[Category: Gow AJ]]
[[Category: Mackay, J P.]]
[[Category: Gu L]]
[[Category: Shi, Y.]]
[[Category: Mackay JP]]
[[Category: Weiss, M J.]]
[[Category: Shi Y]]
[[Category: Zhou, S.]]
[[Category: Weiss MJ]]
[[Category: Ahsp]]
[[Category: Zhou S]]
[[Category: Alpha hemoglobin]]
[[Category: Hemoglobin oxidation and precipitation]]
[[Category: Recognition]]
[[Category: Stabilization of alpha hemoglobin]]
 
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Retrieved from "https://proteopedia.org/1y01"