1w09: Difference between revisions

Revision as of 08:01, 29 July 2008

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File:1w09.png

Template:STRUCTURE 1w09

SOLUTION STRUCTURE OF THE CIS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)SOLUTION STRUCTURE OF THE CIS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)

Template:ABSTRACT PUBMED 15178680

About this StructureAbout this Structure

1W09 is a Single protein structure of sequence from Homo sapiens. Full experimental 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1w09.gif|left|200px]]
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 {{STRUCTURE_1w09|  PDB=1w09  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THE CIS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)'''
+===SOLUTION STRUCTURE OF THE CIS 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15178680}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15178680 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15178680}}
 ==About this Structure==
-W09 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=1W09 OCA].
+W09 is a [[Single protein]] structure of 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].
 ==Reference==
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 [[Category: Chaperone]]
 [[Category: Proline cis/trans isomerization]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:01:08 2008''