1jeb

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[[Image:1jeb.gif|left|200px]]
[[Image:1jeb.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1jeb |SIZE=350|CAPTION= <scene name='initialview01'>1jeb</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1jeb", 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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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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or leave the SCENE parameter empty for the default display.
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|GENE= HBZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1jeb| PDB=1jeb | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeb OCA], [http://www.ebi.ac.uk/pdbsum/1jeb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jeb RCSB]</span>
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'''Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human Zeta2 / Mouse Beta2)'''
'''Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human Zeta2 / Mouse Beta2)'''
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[[Category: Russell, J E.]]
[[Category: Russell, J E.]]
[[Category: Watmough, N J.]]
[[Category: Watmough, N J.]]
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[[Category: oxygen transport]]
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[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:27 2008''
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Revision as of 18:07, 2 May 2008

Image:1jeb.gif

Template:STRUCTURE 1jeb

Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human Zeta2 / Mouse Beta2)


Overview

By using transgenic methodologies, we have produced a number of mouse/human chimeric hemoglobins containing adult mouse and human embryonic globin chains. A detailed analysis of the oxygen binding properties of these proteins identifies the dominant role played by the specific beta-type globin chains in the control of the oxygen binding characteristics. Further analysis traces the origins of these effects to alterations in the properties of the T states of these proteins. The human zeta/mouse beta chimeric protein has been crystallized, and its structure has been determined by X-ray diffraction to a resolution of 2.1 A with R (R(free)) values of 21.6% (24.9%). Close examination of the structure indicates that the subunit interfaces contain contacts which, although different from those present in either the parent human or the parent mouse proteins, retain the overall stabilizing interactions seen in other R state hemoglobins.

About this Structure

1JEB is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function., Kidd RD, Russell JE, Watmough NJ, Baker EN, Brittain T, Biochemistry. 2001 Dec 25;40(51):15669-75. PMID:11747442 Page seeded by OCA on Fri May 2 21:07:03 2008

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