- 関
- amino acid motif
WordNet
- a design or figure that consists of recurring shapes or colors, as in architecture or decoration (同)motive
- a theme that is repeated or elaborated in a piece of music (同)motive
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/11/14 18:40:26」(JST)
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In a chain-like biological molecule, such as a protein or nucleic acid, a structural motif is a supersecondary structure, which also appears in a variety of other molecules. Motifs do not allow us to predict the biological functions: they are found in proteins and enzymes with dissimilar functions.
Because the relationship between primary structure and tertiary structure is not straightforward, two biopolymers may share the same motif yet lack appreciable primary structure similarity. In other words, a structural motif does not have to be associated with a sequence motif. Also, the existence of a sequence motif does not necessarily imply a distinctive structure. In most DNA motifs, for example, it is assumed that the DNA of that sequence does not deviate from the normal "double helical" structure.
Contents
- 1 Structural motifs in proteins
- 2 See also
- 3 References
- 4 Further reading
Structural motifs in proteins[edit]
In proteins, structure motifs usually consist of just a few elements; e.g., the 'helix-turn-helix' has just three. Note that , while the spatial sequence of elements is the same in all instances of a motif, they may be encoded in any order within the underlying gene. Protein structural motifs often include loops of variable length and unspecified structure, which in effect create the "slack" necessary to bring together in space two elements that are not encoded by immediately adjacent DNA sequences in a gene. Note also that, even when two genes encode secondary structural elements of a motif in the same order, they may specify somewhat different sequences of amino acids. This is true not only because of the complicated relationship between tertiary and primary structure but also because the size of the elements varies from one protein and the next.
Extremely common. Two antiparallel beta strands connected by a tight turn of a few amino acids between them.
4 beta strands folded over into a sandwich shape.
a loop in which the residues that make up the beginning and end of the loop are very close together.
Consists of alpha helices bound by a looping stretch of amino acids. This motif is seen in transcription factors.
Two beta strands with an alpha helix end folded over to bind a zinc ion. Important in DNA binding proteins.
See also: structural domain
See also[edit]
- Motif domain
- Sequence motif
- Short linear motif
References[edit]
- PROSITE Database of protein families and domains
- SCOP Structural classification of Proteins
- CATH Class Architecture Topology Homology
- FSSP FSSP
- PASS2 PASS2 - Protein Alignments as Structural Superfamilies
- SMoS SMoS - Database of Structural Motifs of Superfamily
- S4 S4: Server for Super-Secondary Structure Motif Mining
Further reading[edit]
- Chiang YS, Gelfand TI, Kister AE, Gelfand IM (2007). "New classification of supersecondary structures of sandwich-like proteins uncovers strict patterns of strand assemblage.". Proteins. 68 (4): 915–921. doi:10.1002/prot.21473. PMID 17557333.
UpToDate Contents
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English Journal
- Prostaglandin E2-Dependent Phosphorylation of RAS Inhibition 1 (RIN1) at Ser 291 and 292 Inhibits Transforming Growth Factor-β-Induced RAS Activation Pathway in Human Synovial Fibroblasts: Role in Cell Migration.
- Gerarduzzi C1,2, He Q3, Zhai B4, Antoniou J5, Di Battista JA3.
- Journal of cellular physiology.J Cell Physiol.2017 Jan;232(1):202-15. doi: 10.1002/jcp.25412. Epub 2016 May 26.
- Prostaglandin E2 (PGE2 )-stimulated G-protein-coupled receptor (GPCR) activation inhibits pro-fibrotic TGFβ-dependent stimulation of human fibroblast to myofibroblast transition (FMT), though the precise molecular mechanisms are not fully understood. In the present study, we describe the PGE2 -depe
- PMID 27137893
- Split-Intein Triggered Protein Hydrogels.
- Ramirez MA1, Chen Z2,3.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2017;1495:161-171.
- Proteins are nature's building blocks and indispensable in living organisms. Protein-based hydrogels have a wide variety of applications in research and biotechnology. In this chapter, we describe an intein-mediated protein hydrogel that utilizes two synthetic soluble protein block copolymers, each
- PMID 27714616
- Recombinant Expression of Cyclotides Using Split Inteins.
- Jagadish K1, Camarero JA2,3.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2017;1495:41-55.
- Cyclotides are fascinating microproteins (≈30 residues long) present in several families of plants that share a unique head-to-tail circular knotted topology of three disulfide bridges, with one disulfide penetrating through a macrocycle formed by the two other disulfides and inter-connecting pept
- PMID 27714609
Japanese Journal
- Susceptibility of muridae cell lines to ecotropic murine leukemia virus and the cationic amino acid transporter 1 viral receptor sequences: implications for evolution of the viral receptor
- Kakoki Katsura,Shinohara Akio,Izumida Mai,Koizumi Yosuke,Honda Eri,Kato Goro,Igawa Tsukasa,Sakai Hideki,Hayashi Hideki,Matsuyama Toshifumi,Morita Tetsuo,Koshimoto Chihiro,Kubo Yoshinao
- Virus Genes 48(3), 448-456, 2014-06
- … Comparison of amino acid sequences between the rat and mouse CAT1s shows amino acid insertions in the rat protein near the Eco-MLV-binding motif. … In contrast, tunicamycin treatment of mink and human cells does not elevate the infection, because their CAT1s do not have the Eco-MLV-binding motif. …
- NAID 120005451801
- Localization of Daucus carota NMCP1 to the nuclear periphery: the role of the N-terminal region and an NLS-linked sequence motif, RYNLRR, in the tail domain
- Kimura Yuta,Fujino Kaien,Ogawa Kana,Masuda Kiyoshi
- Frontiers in plant science 5, 2014-02-26
- … NMCP1 is a protein, first identified in Daucus carota cells, that localizes exclusively to the nuclear periphery in interphase cells. … We identified the functional NLS of DcNMCP1 (carrot NMCP1) and determined the protein regions required for localizing to the nuclear periphery using EGFP-fused constructs transiently expressed in Apium graveolens epidermal cells. …
- NAID 120005425330
- Functional Analysis of Light-harvesting-like Protein 3 (LIL3) and Its Light-harvesting Chlorophyll-binding Motif in Arabidopsis
- Takahashi Kaori,Takabayashi Atsushi,Tanaka Ayumi,Tanaka Ryouichi
- Journal of biological chemistry 289(2), 987-999, 2014-01-10
- … LHC contains a characteristic sequence motif, termed LHC motif, consisting of 25-30 mostly hydrophobic amino acids. … This motif is shared by a number of transmembrane proteins from oxygenic photoautotrophs that are termed light-harvesting-like (LIL) proteins. … To gain insights into the functions of LIL proteins and their LHC motifs, we functionally characterized a plant LIL protein, LIL3. …
- NAID 120005418077
Related Links
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