Band 4.1
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| Erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)
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| Image:PBB Protein EPB41 image.jpg | ||||||||||||||||||||||||||||||||||||||
| PDB rendering based on 1gg3. | ||||||||||||||||||||||||||||||||||||||
| Available structures: For the file format that describes the 3D structures of molecules found in the Protein Data Bank, see Protein Data Bank (file format).
The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. These data, typically obtained by X-ray crystallography or NMR spectroscopy, are submitted by biologists and biochemists from around the world, are released into the public domain, and can be accessed for free. HistoryFounded in 1971 by Drs. Edgar Meyer and Walter Hamilton Brookhaven National Laboratory, management of the Protein Data Bank was transferred in 1998 to members of the Research Collaboratory for Structural Bioinformatics (RCSB). The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. The founding members are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan). The BMRB (USA) group joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single Protein Data Bank Archive of macromolecular structural data that is freely and publicly available to the global community. The PDB is a key resource in structural biology and is critical to more recent work in structural genomics. Countless derived databases and projects have been developed to integrate and classify the PDB in terms of protein structure, protein function and protein evolution. GrowthWhen the PDB was originally founded it contained just 7 protein structures. Since then it has undergone an approximate exponential growth in the number of structures, which does not show any sign of falling off. The growth rate of the PDB has been the subject of fairly extensive analysis. ContentsAs of 26 September, 2006, the database contained 39,051 released atomic coordinate entries (or "structures"), 35,767 of that proteins, the rest being nucleic acids, nucleic acid-protein complexes, and a few other molecules. About 5,000 new structures are released each year. Data are stored in the mmCIF format specifically developed for the purpose. Note that the database stores information about the exact location of all atoms in a large biomolecule (although, usually without the hydrogen atoms, as their positions are more of a statistical estimate); if one is only interested in sequence data, i.e. the list of amino acids making up a particular protein or the list of nucleotides making up a particular nucleic acid, the much larger databases from Swiss-Prot and the International Nucleotide Sequence Database Collaboration should be used. StatisticsAs of 11 September, 2007, the "PDB Holdings List" at RCSB reported the following statistics:
Note that theoretical models are no longer accepted in the PDB. 22461 structures in the PDB have a structure factor file. 3138 structures in the PDB have an NMR restraint file. The current breakdown of holdings is updated weekly. File formatThrough the years the PDB file format has undergone many, many changes and revisions. Its original format was dictated by the width of computer punch cards.
This legacy format has caused many problems with the format, and consequently there are 'clean-up' projects; The MMDB uses ASN.1 (and an XML conversion of this format). The wwPDB members RCSB PDB, MSD-EBI, and PDBj are working together to make the data uniform across the archive. Some believe this to be desirable; others argue that, without a universal repository of information (i.e., a common dictionary), it is not possible to draw comparisons. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID. This should not be used as an identifier for biomolecules, since often several structures for the same molecule (in different environments or conformations) are contained in PDB with different PDB IDs. If a biologist submits structure data for a protein or nucleic acid, wwPDB staff reviews and annotates the entry. The data are then automatically checked for plausibility. The source code for this validation software has been released for free. The main data base accepts only experimentally derived structures, and not theoretically predicted ones (see protein structure prediction). Various funding agencies and scientific journals now require scientists to submit their structure data to PDB. Viewing the dataThe structural data can be used to visualize the biomolecules with appropriate software, such as VMD, RasMol, PyMOL, Jmol, MDL Chime, QuteMol, web browser VRML plugin or any web-based software designed to visualize and analyse the protein structures such as STING. A recent desktop software addition is Sirius. The RCSB PDB website also contains resources for education, structural genomics, and related software. ReferencesPrinted
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| Identifiers | ||||||||||||||||||||||||||||||||||||||
| Symbol(s) | EPB41; 4.1R; EL1; HE | |||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 130500 MGI: 95401 Homologene: 44324 | |||||||||||||||||||||||||||||||||||||
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| RNA expression pattern | ||||||||||||||||||||||||||||||||||||||
| Image:PBB GE EPB41 207793 s at tn.png Image:PBB GE EPB41 214530 x at tn.png | ||||||||||||||||||||||||||||||||||||||
| Orthologs | ||||||||||||||||||||||||||||||||||||||
| Human | Mouse | |||||||||||||||||||||||||||||||||||||
| Entrez | 2035 | 269587 | ||||||||||||||||||||||||||||||||||||
| Ensembl | ENSG00000159023 | ENSMUSG00000028906 | ||||||||||||||||||||||||||||||||||||
| Uniprot | P11171 | Q3U0G7 | ||||||||||||||||||||||||||||||||||||
| Refseq | NM_004437 (mRNA) NP_004428 (protein) | NM_183428 (mRNA) NP_906273 (protein) | ||||||||||||||||||||||||||||||||||||
| Location | Chr 1: 29.09 - 29.32 Mb | Chr 4: 131.2 - 131.35 Mb | ||||||||||||||||||||||||||||||||||||
| Pubmed search | [5] | [6] | ||||||||||||||||||||||||||||||||||||
Erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked), also known as EPB41, is a human gene.
Elliptocytosis is a hematologic disorder characterized by elliptically shaped erythrocytes and a variable degree of hemolytic anemia. Inherited as an autosomal dominant, elliptocytosis results from mutation in any one of several genes encoding proteins of the red cell membrane skeleton. The form discussed here is the one found in the 1950s to be linked to Rh blood group and more recently shown to be caused by a defect in protein 4.1. 'Rh-unlinked' forms of elliptocytosis are caused by mutation in the alpha-spectrin gene (MIM 182860), the beta-spectrin gene (MIM 182870), or the band 3 gene (MIM 109270).[supplied by OMIM][1]
Band 4.1 is a protein associated with the cytoskeleton of the red blood cell.
See also
References
Further reading
- Conboy JG (1993). "Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells.". Semin. Hematol. 30 (1): 58-73. PMID 8434260.
- Calinisan V, Gravem D, Chen RP, et al. (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium.". Front. Biosci. 11: 1646-66. PMID 16368544.
- Dalla Venezia N, Gilsanz F, Alloisio N, et al. (1992). "Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene.". J. Clin. Invest. 90 (5): 1713-7. PMID 1430200.
- Jöns T, Drenckhahn D (1992). "Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger.". EMBO J. 11 (8): 2863-7. PMID 1639060.
- Subrahmanyam G, Bertics PJ, Anderson RA (1991). "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro.". Proc. Natl. Acad. Sci. U.S.A. 88 (12): 5222-6. PMID 1647028.
- Conboy JG, Chan JY, Chasis JA, et al. (1991). "Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1.". J. Biol. Chem. 266 (13): 8273-80. PMID 2022644.
- Horne WC, Prinz WC, Tang EK (1990). "Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1.". Biochim. Biophys. Acta 1055 (1): 87-92. PMID 2171679.
- Conboy J, Marchesi S, Kim R, et al. (1990). "Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements.". J. Clin. Invest. 86 (2): 524-30. PMID 2384598.
- Inaba M, Maede Y (1989). "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.". J. Biol. Chem. 264 (30): 18149-55. PMID 2808371.
- Korsgren C, Cohen CM (1988). "Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3.". J. Biol. Chem. 263 (21): 10212-8. PMID 2968981.
- Conboy JG, Chan J, Mohandas N, Kan YW (1988). "Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells.". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9062-5. PMID 3194408.
- Tang TK, Leto TL, Marchesi VT, Benz EJ (1989). "Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues.". Adv. Exp. Med. Biol. 241: 81-95. PMID 3223413.
- Tang TK, Leto TL, Correas I, et al. (1988). "Selective expression of an erythroid-specific isoform of protein 4.1.". Proc. Natl. Acad. Sci. U.S.A. 85 (11): 3713-7. PMID 3375238.
- Conboy J, Kan YW, Shohet SB, Mohandas N (1987). "Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton.". Proc. Natl. Acad. Sci. U.S.A. 83 (24): 9512-6. PMID 3467321.
- Correas I, Speicher DW, Marchesi VT (1986). "Structure of the spectrin-actin binding site of erythrocyte protein 4.1.". J. Biol. Chem. 261 (28): 13362-6. PMID 3531202.
- Tchernia G, Mohandas N, Shohet SB (1981). "Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability.". J. Clin. Invest. 68 (2): 454-60. PMID 6894932.
- Schischmanoff PO, Winardi R, Discher DE, et al. (1995). "Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding.". J. Biol. Chem. 270 (36): 21243-50. PMID 7673158.
- Lue RA, Marfatia SM, Branton D, Chishti AH (1994). "Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1.". Proc. Natl. Acad. Sci. U.S.A. 91 (21): 9818-22. PMID 7937897.
- Conboy JG, Chasis JA, Winardi R, et al. (1993). "An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells.". J. Clin. Invest. 91 (1): 77-82. PMID 8423235.
External links
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
