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| [[Image:1hyn.gif|left|200px]] | | {{Seed}} |
| | [[Image:1hyn.png|left|200px]] |
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| {{STRUCTURE_1hyn| PDB=1hyn | SCENE= }} | | {{STRUCTURE_1hyn| PDB=1hyn | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN'''
| | ===CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN=== |
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| ==Overview==
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| The red blood cell membrane (RBCM) is a primary model for animal cell plasma membranes. One of its major organizing centers is the cytoplasmic domain of band 3 (cdb3), which links multiple proteins to the membrane. Included among its peripheral protein ligands are ankyrin (the major bridge to the spectrin-actin skeleton), protein 4. 1, protein 4.2, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphofructokinase, deoxyhemoglobin, p72syk protein tyrosine kinase, and hemichromes. The crystal structure of cdb3 is reported at 0.26 nm (2.6 A) resolution. A tight symmetric dimer is formed by cdb3; it is stabilized by interlocked dimerization arms contributed by both monomers. Each subunit also includes a larger peripheral protein binding domain with an alpha(+) beta-fold. The binding sites of several peripheral proteins are localized in the structure, and the nature of the major conformational change that regulates membrane-skeletal interactions is evaluated. An improved structural definition of the protein network at the inner surface of the RBCM is now possible. | | The line below this paragraph, {{ABSTRACT_PUBMED_11049968}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11049968 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11049968}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zhang, D.]] | | [[Category: Zhang, D.]] |
| [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:22:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:08:18 2008'' |