1w0a
From Proteopedia
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| - | [[Image:1w0a.gif|left|200px]]<br /> | + | [[Image:1w0a.gif|left|200px]]<br /><applet load="1w0a" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1w0a" size=" | + | |
caption="1w0a" /> | caption="1w0a" /> | ||
'''SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)'''<br /> | '''SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1W0A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1W0A is a [http://en.wikipedia.org/wiki/Single_protein 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=1W0A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Allen, M | + | [[Category: Allen, M D.]] |
[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
| - | [[Category: Perez-Canadillas, J | + | [[Category: Perez-Canadillas, J M.]] |
| - | [[Category: Rutherford, T | + | [[Category: Rutherford, T J.]] |
| - | [[Category: Santiveri, C | + | [[Category: Santiveri, C M.]] |
| - | [[Category: Vadivelu, M | + | [[Category: Vadivelu, M K.]] |
| - | [[Category: Watkins, N | + | [[Category: Watkins, N A.]] |
[[Category: ahsp nmr structure]] | [[Category: ahsp nmr structure]] | ||
[[Category: alpha-hemoglobin binding]] | [[Category: alpha-hemoglobin binding]] | ||
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[[Category: proline cis/trans isomerization]] | [[Category: proline cis/trans isomerization]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:08 2008'' |
Revision as of 13:39, 21 February 2008
|
SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)
Overview
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.
About this Structure
1W0A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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