1hyn
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyn OCA], [http://www.ebi.ac.uk/pdbsum/1hyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hyn RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
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 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Blood group, Diego OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Blood group, Froese , OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Blood group, Waldner OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Blood group, Wright OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Diabetes insipidus, nephrogenic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300538 300538]], Hemolytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Malaria, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Nephrogenic syndrome of inappropriate antidiuresis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300538 300538]], Ovalocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Renal tubular acidosis, distal, AD OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Renal tubular acidosis, distal, AR OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Spherocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 31: | Line 31: | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:05 2008'' |
Revision as of 18:12, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN
Overview
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.
About this Structure
1HYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3., Zhang D, Kiyatkin A, Bolin JT, Low PS, Blood. 2000 Nov 1;96(9):2925-33. PMID:11049968
Page seeded by OCA on Sun Mar 30 21:12:05 2008
