1w09: Difference between revisions

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[[Image:1w09.png|left|200px]]


{{STRUCTURE_1w09| PDB=1w09 |  SCENE= }}
==Solution structure of the cis form of the human alpha-hemoglobin stabilizing protein (AHSP)==
<StructureSection load='1w09' size='340' side='right'caption='[[1w09]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1w09]] 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=1W09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W09 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1w09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w09 OCA], [https://pdbe.org/1w09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w09 RCSB], [https://www.ebi.ac.uk/pdbsum/1w09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w09 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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy. The protein native state shows conformational heterogeneity attributable to the isomerization of the peptide bond preceding a conserved proline residue. The two equally populated cis and trans forms both adopt an elongated antiparallel three alpha-helix bundle fold but display major differences in the loop between the first two helices and at the C terminus of helix 3. Proline to alanine single point mutation of the residue Pro-30 prevents the cis/trans isomerization. The structure of the P30A mutant is similar to the structure of the trans form of AHSP in the loop 1 region. Both the wild-type AHSP and the P30A mutant bind to alpha-hemoglobin, and the wild-type conformational heterogeneity is quenched upon complex formation, suggesting that just one conformation is the active form. Changes in chemical shift observed upon complex formation identify a binding interface comprising the C terminus of helix 1, the loop 1, and the N terminus of helix 2, with the exposed residues Phe-47 and Tyr-51 being attractive targets for molecular recognition. The characteristics of this interface suggest that AHSP binds at the intradimer alpha1beta1 interface in tetrameric HbA.


===SOLUTION STRUCTURE OF THE CIS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)===
NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.,Santiveri CM, Perez-Canadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M J Biol Chem. 2004 Aug 13;279(33):34963-70. Epub 2004 Jun 3. PMID:15178680<ref>PMID:15178680</ref>


{{ABSTRACT_PUBMED_15178680}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1w09" style="background-color:#fffaf0;"></div>
[[1w09]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W09 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:015178680</ref><references group="xtra"/>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Allen, M D.]]
[[Category: Large Structures]]
[[Category: Bycroft, M.]]
[[Category: Allen MD]]
[[Category: Perez-Canadillas, J M.]]
[[Category: Bycroft M]]
[[Category: Rutherford, T J.]]
[[Category: Perez-Canadillas JM]]
[[Category: Santiveri, C M.]]
[[Category: Rutherford TJ]]
[[Category: Vadivelu, M K.]]
[[Category: Santiveri CM]]
[[Category: Watkins, N A.]]
[[Category: Vadivelu MK]]
[[Category: Ahsp nmr structure]]
[[Category: Watkins NA]]
[[Category: Alpha-hemoglobin binding]]
[[Category: Alpha-thalassaemia]]
[[Category: Chaperone]]
[[Category: Proline cis/trans isomerization]]

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