1xz2

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[[Image:1xz2.gif|left|200px]]
[[Image:1xz2.gif|left|200px]]
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{{Structure
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|PDB= 1xz2 |SIZE=350|CAPTION= <scene name='initialview01'>1xz2</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1xz2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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{{STRUCTURE_1xz2| PDB=1xz2 | SCENE= }}
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|RELATEDENTRY=[[1rq3|1RQ3]], [[1xye|1XYE]], [[1xz4|1XZ4]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xz2 OCA], [http://www.ebi.ac.uk/pdbsum/1xz2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xz2 RCSB]</span>
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}}
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'''wild-type hemoglobin deoxy no-salt'''
'''wild-type hemoglobin deoxy no-salt'''
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[[Category: Rogers, P H.]]
[[Category: Rogers, P H.]]
[[Category: Wierzba, A.]]
[[Category: Wierzba, A.]]
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[[Category: globin]]
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[[Category: Globin]]
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[[Category: hemoglobin]]
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[[Category: Hemoglobin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:41:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:56:36 2008''
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Revision as of 12:41, 3 May 2008

Image:1xz2.gif

Template:STRUCTURE 1xz2

wild-type hemoglobin deoxy no-salt


Overview

Previous mutational studies on Tyr42alpha variants as well as the current studies on the mutant hemoglobin alphaY42A show that the intersubunit interactions associated with Tyr42alpha significantly stabilize the alpha1beta2 interface of the quaternary-T deoxyhemoglobin tetramer. However, crystallographic studies, UV and visible resonance Raman spectroscopy, CO combination kinetic measurements, and oxygen binding measurements on alphaY42A show that the intersubunit interactions formed by Tyr42alpha have only a modest influence on the structural properties and ligand affinity of the deoxyhemoglobin tetramer. Therefore, the alpha1beta2 interface interactions associated with Tyr42alpha do not contribute significantly to the quaternary constraints that are responsible for the low oxygen affinity of deoxyhemoglobin. The slight increase in the ligand affinity of deoxy alphaY42A correlates with small, mutation-induced structural changes that perturb the environment of Trp37beta, a critical region of the quaternary-T alpha1beta2 interface that has been shown to be the major source of quaternary constraint in deoxyhemoglobin.

About this Structure

1XZ2 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin., Kavanaugh JS, Rogers PH, Arnone A, Hui HL, Wierzba A, DeYoung A, Kwiatkowski LD, Noble RW, Juszczak LJ, Peterson ES, Friedman JM, Biochemistry. 2005 Mar 15;44(10):3806-20. PMID:15751957 Page seeded by OCA on Sat May 3 15:41:13 2008

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OCA

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