Sterile Alpha Motif
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Sterile Alpha Motif
In molecular biology, the protein domain Sterile alpha motif (or SAM) is a putative protein interaction module present in a wide variety of proteins involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms. SAM domains have been shown to homo- and hetero-oligomerise, forming multiple self-association architectures and also binding to various non-SAM domain-containing proteins, nevertheless with a low affinity constant. SAM domains also appear to possess the ability to bind RNA. Smaug, a protein that helps to establish a morphogen gradient in ''Drosophila'' embryos by repressing the translation of nanos (nos) mRNA, binds to the 3' untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain, which could be the RNA-binding surface. This electropositive potential is un ...
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Molecular Biology
Molecular biology is the branch of biology that seeks to understand the molecular basis of biological activity in and between cells, including biomolecular synthesis, modification, mechanisms, and interactions. The study of chemical and physical structure of biological macromolecules is known as molecular biology. Molecular biology was first described as an approach focused on the underpinnings of biological phenomena - uncovering the structures of biological molecules as well as their interactions, and how these interactions explain observations of classical biology. In 1945 the term molecular biology was used by physicist William Astbury. In 1953 Francis Crick, James Watson, Rosalind Franklin, and colleagues, working at Medical Research Council unit, Cavendish laboratory, Cambridge (now the MRC Laboratory of Molecular Biology), made a double helix model of DNA which changed the entire research scenario. They proposed the DNA structure based on previous research done by Ro ...
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Alpha Helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. Discovery In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈. Astb ...
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CENTD1
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the ''ARAP2'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... Function The protein encoded by this gene contains ARF-GAP, RHO-GAP, ankyrin repeat, RAS-associating, and pleckstrin homology domains. This protein lacks the predicted catalytic arginine in the RHO-GAP domain and is therefore unlikely to have RHO-GAP activity. While the encoded protein does contain a sterile alpha motif (SAM) commonly found in some signaling molecules, the function of the protein has not been determined. Two transcript variants encoding different isoforms have been found for this gene. References External links * Further reading

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ANKS4B
Ankyrin repeat and sterile alpha motif domain containing 4B is a protein that in humans is encoded by the ''ANKS4B'' gene. The gene is also known as ''HARP'' (Harmonin-interacting, ankyrin repeat-containing protein). Ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. Model organisms Model organisms have been used in the study of ANKS4B function. A conditional knockout mouse line, called ''Anks4btm2a(EUCOMM)Wtsi'' was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out on mutant In biology, and especially in genetics, a mutant is an organism or a new genetic character arising or resulting from an instance of mutati ...
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ANKS1B
Ankyrin repeat and sterile alpha motif domain-containing protein 1B is a protein that in humans is encoded by the ''ANKS1B'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... References External links * * Further reading

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ANKS1A
Ankyrin repeat and SAM domain-containing protein 1A (ANKS1A), also known as ODIN, is a protein that in humans is encoded by the ''ANKS1A'' gene on chromosome 6. It is ubiquitously expressed in many tissues and cell types. ODIN is known to regulate the epidermal growth factor receptor (EGFR) and EphA receptor signaling pathways. As a Src family kinase target, ODIN has been implicated in the development of cancer. The ''ANKS1A'' gene also contains one of 27 SNPs associated with increased risk of coronary artery disease. Structure Gene The ''ANKS1A'' gene resides on chromosome 6 at the band 6p21.31 and includes 29 exons. This gene produces 2 isoforms through alternative splicing. Protein ODIN is a member of the ankyrin repeat and sterile alpha motif domain-containing (ANKS) family and contains 6 ankyrin repeats, 1 phosphotyrosine binding (PTD) domain, and 2 tandem sterile alpha motif (SAM) domains. The first SAM domain binds to the SAM domain of the EphA2 receptor by adop ...
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