1w0a: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0a RCSB], [http://www.ebi.ac.uk/pdbsum/1w0a PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0a RCSB], [http://www.ebi.ac.uk/pdbsum/1w0a PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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 == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Allen, M D | [[Category: Allen, M D]] | ||
[[Category: Bycroft, M | [[Category: Bycroft, M]] | ||
[[Category: Perez-Canadillas, J M | [[Category: Perez-Canadillas, J M]] | ||
[[Category: Rutherford, T J | [[Category: Rutherford, T J]] | ||
[[Category: Santiveri, C M | [[Category: Santiveri, C M]] | ||
[[Category: Vadivelu, M K | [[Category: Vadivelu, M K]] | ||
[[Category: Watkins, N A | [[Category: Watkins, N A]] | ||
[[Category: Ahsp nmr structure]] | [[Category: Ahsp nmr structure]] | ||
[[Category: Alpha-hemoglobin binding]] | [[Category: Alpha-hemoglobin binding]] | ||
Revision as of 19:37, 24 December 2014
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
Function[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.[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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