1jeb

From Proteopedia

Revision as of 15:33, 12 November 2007

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 with ACE, HEM and CMO as ligands. 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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