1w0a: Difference between revisions
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==Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)== | ==Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)== | ||
<StructureSection load='1w0a' size='340' side='right'caption='[[1w0a | <StructureSection load='1w0a' size='340' side='right'caption='[[1w0a]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w0a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1w0a]] 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=1W0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0A FirstGlance]. <br> | ||
</td></tr><tr id=' | </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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0a OCA], [https://pdbe.org/1w0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0a RCSB], [https://www.ebi.ac.uk/pdbsum/1w0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Allen | [[Category: Allen MD]] | ||
[[Category: Bycroft | [[Category: Bycroft M]] | ||
[[Category: Perez-Canadillas | [[Category: Perez-Canadillas JM]] | ||
[[Category: Rutherford | [[Category: Rutherford TJ]] | ||
[[Category: Santiveri | [[Category: Santiveri CM]] | ||
[[Category: Vadivelu | [[Category: Vadivelu MK]] | ||
[[Category: Watkins | [[Category: Watkins NA]] | ||
Latest revision as of 13:29, 16 August 2023
Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)
Structural highlights
FunctionAHSP_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.[1] Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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