1jeb

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[[Image:1jeb.gif|left|200px]]
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{{Seed}}
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[[Image:1jeb.png|left|200px]]
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{{STRUCTURE_1jeb| PDB=1jeb | SCENE= }}
{{STRUCTURE_1jeb| PDB=1jeb | SCENE= }}
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'''Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human Zeta2 / Mouse Beta2)'''
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===Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human Zeta2 / Mouse Beta2)===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11747442}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11747442 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11747442}}
==About this Structure==
==About this Structure==
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[[Category: Watmough, N J.]]
[[Category: Watmough, N J.]]
[[Category: Oxygen transport]]
[[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 Tue Jul 1 20:06:44 2008''

Revision as of 17:06, 1 July 2008

Image:1jeb.png

Template:STRUCTURE 1jeb

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

Template:ABSTRACT PUBMED 11747442

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

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