1xzy

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[[Image:1xzy.gif|left|200px]]<br />
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[[Image:1xzy.jpg|left|200px]]<br /><applet load="1xzy" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1xzy" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1xzy" />
caption="1xzy" />
'''Solution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)'''<br />
'''Solution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)'''<br />
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==About this Structure==
==About this Structure==
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1XZY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XZY OCA].
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1XZY 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=1XZY OCA].
==Reference==
==Reference==
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[[Category: three-helix bundle]]
[[Category: three-helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:12:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:10:59 2008''

Revision as of 15:10, 15 February 2008


1xzy

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Solution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)

Overview

Hemoglobin A (HbA), the oxygen delivery system in humans, comprises two, alpha and two beta subunits. Free alpha-hemoglobin (alphaHb) is unstable, and its precipitation contributes to the pathophysiology of beta, thalassemia. In erythrocytes, the alpha-hemoglobin stabilizing protein, (AHSP) binds alphaHb and inhibits its precipitation. The crystal structure, of AHSP bound to Fe(II)-alphaHb reveals that AHSP specifically recognizes, the G and H helices of alphaHb through a hydrophobic interface that, largely recapitulates the alpha1-beta1 interface of hemoglobin. The, AHSP-alphaHb interactions are extensive but suboptimal, explaining why, beta-hemoglobin can competitively displace AHSP to form HbA. Remarkably, the Fe(II)-heme group in AHSP bound alphaHb is coordinated by the distal, but not the proximal histidine. Importantly, binding to AHSP facilitates, the conversion of oxy-alphaHb to a deoxygenated, oxidized [Fe(III)], nonreactive form in which all six coordinate positions are occupied. These, observations reveal the molecular mechanisms by which AHSP stabilizes free, alphaHb.

About this Structure

1XZY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin., Feng L, Gell DA, Zhou S, Gu L, Kong Y, Li J, Hu M, Yan N, Lee C, Rich AM, Armstrong RS, Lay PA, Gow AJ, Weiss MJ, Mackay JP, Shi Y, Cell. 2004 Nov 24;119(5):629-40. PMID:15550245

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