1w0a: Difference between revisions
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'''SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)''' | {{Structure | ||
|PDB= 1w0a |SIZE=350|CAPTION= <scene name='initialview01'>1w0a</scene> | |||
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'''SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1W0A is a [ | 1W0A is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15178680 15178680] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: proline cis/trans isomerization]] | [[Category: proline cis/trans isomerization]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:24 2008'' | ||
Revision as of 15:50, 20 March 2008
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SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)
OverviewOverview
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 StructureAbout this Structure
1W0A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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