- 関
- transmembrane helices
WordNet
- a curve that lies on the surface of a cylinder or cone and cuts the element at a constant angle (同)spiral
- type genus of the family Helicidae (同)genus Helix
PrepTutorEJDIC
- らせん / らせん形のもの
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/10/19 01:21:17」(JST)
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Transmembrane segment usually denotes a single transmembrane alpha helix of a transmembrane protein, also known as an integral protein.[1] More broadly, a transmembrane segment is any three-dimensional protein structure which is thermodynamically stable in a membrane. This may be a single alpha helix, a transmembrane beta barrel, a beta-helix of gramicidin A, or any other structure. Transmembrane helices are usually about 20 amino acids in length.
Identification of transmembrane helices
Transmembrane helices are visible in structures of membrane proteins determined by X-ray diffraction. They may also be predicted on the basis of hydrophobicity scales. Because the interior of the bilayer and the interiors of most proteins of known structure are hydrophobic, it is presumed to be a requirement of the amino acids that span a membrane that they be hydrophobic as well. However, membrane pumps and ion channels also contain numerous charged and polar residues within the generally non-polar transmembrane segments.
Using hydrophobicity analysis to predict transmembrane helices enables a prediction in turn of the "transmembrane topology" of a protein; i.e. prediction of what parts of it protrude into the cell, what parts protrude out, and how many times the protein chain crosses the membrane. Such prediction methods are commonly applied with a limited success.
Online transmembrane prediction algorithm servers are listed by Expasy [1] under Topology prediction. The resulting predictions often differ and should be used with caution.
References
- ^ http://www.cell.com/abstract/S0092-8674%2810%2900612-4#Introduction
UpToDate Contents
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English Journal
- One motif to bind them: A small-XXX-small motif affects transmembrane domain 1 oligomerization, function, localization, and cross-talk between two yeast GPCRs.
- Lock A1, Forfar R2, Weston C2, Bowsher L3, Upton GJ4, Reynolds CA4, Ladds G5, Dixon AM6.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Dec;1838(12):3036-51. doi: 10.1016/j.bbamem.2014.08.019. Epub 2014 Aug 23.
- G protein-coupled receptors (GPCRs) are the largest family of cell-surface receptors in mammals and facilitate a range of physiological responses triggered by a variety of ligands. GPCRs were thought to function as monomers, however it is now accepted that GPCR homo- and hetero-oligomers also exist
- PMID 25157670
- Molecular and structural transmembrane determinants critical for embedding claudin-5 into tight junctions reveal a distinct four-helix bundle arrangement.
- Rossa J1, Protze J1, Kern C1, Piontek A1, Günzel D2, Krause G1, Piontek J2.
- The Biochemical journal.Biochem J.2014 Nov 15;464(1):49-60. doi: 10.1042/BJ20140431.
- The mechanism of TJ (tight junction) assembly and the structure of TJ strand-forming Cldns (claudins) are unclear. To identify determinants of assembly of blood-brain barrier-related Cldn3 and Cldn5, chimaeric mutants were analysed by cellular reconstitution of TJ strands and live-cell imaging. On t
- PMID 25174580
- Second Transmembrane Helix (M2) and Long Range Coupling in Ca2+-ATPase.
- Daiho T1, Yamasaki K2, Danko S2, Suzuki H2.
- The Journal of biological chemistry.J Biol Chem.2014 Nov 7;289(45):31241-52. doi: 10.1074/jbc.M114.584086. Epub 2014 Sep 22.
- The actuator (A) domain of sarco(endo)plasmic reticulum Ca(2+)-ATPase not only plays a catalytic role but also undergoes large rotational movements that influence the distant transport sites through connections with transmembrane helices M1 and M2. Here we explore the importance of long helix M2 and
- PMID 25246522
Japanese Journal
- Lipophobic Interaction : Lipid-Induced Association of Transmembrane Helices
- YANO Yoshiaki,YAMAMOTO Arisa,OGURA Mai,MATSUZAKI Katsumi
- Peptide science : proceedings of the ... Japanese Peptide Symposium 2011, 71-72, 2012-03-01
- NAID 10030204026
- Mechanism of Inverse Agonist Action of Sarpogrelate at the Constitutively Active Mutant of Human 5-HT2A Receptor Revealed by Molecular Modeling
- Hossain Murad,Muntasir Habib Abul,Ishiguro Masaji,Bhuiyan Mohiuddin Ahmed,Rashid Mamunur,Sugihara Takumichi,Nagatomo Takafumi
- Biological and Pharmaceutical Bulletin 35(9), 1553-1559, 2012
- … Our model shows that mutation (C322K) of 5-HT2AR causes electronic repulsion between positively charged Arg173(3.50) and Lys322(6.34) residues resulting outward movement of the C-terminus of transmembrane helix (TMH) III. …
- NAID 130001872084
- 3B0924 膜貫通ヘリックスの膜分配・自己会合の熱力学 : ホスファチジルエタノールアミンによる疎脂性相互作用(3B 膜蛋白質2,日本生物物理学会第49回年会)
- Yano Yoshiaki,Yamamoto Arisa,Ogura Mai,Matsuzaki Katsumi
- 生物物理 51(SUPPLEMENT_1), S108, 2011-08-15
- NAID 110008903386
Related Links
- Protein with at least one transmembrane helical domain, a membrane-spanning domain with an hydrogen-bonded helical configuration, including alpha-, 3-10-, and pi-helices. The transmembrane alpha-helix is very common, while the ...
- Prediction of transmembrane helices in proteins Instructions SUBMISSION Submission of a local file in FASTA format (HTML 3.0 or higher) OR by pasting sequence(s) in FASTA format: Output format: Extensive, with graphics ...
★リンクテーブル★
[★]
- 英
- transmembrane helix
- 関
- 膜貫通ドメイン
[★]
膜貫通ヘリックス
- 関
- transmembrane helix
[★]
- 関
- helical、helices、snail、spiral
[★]
- 関
- membrane-spanning、TM、transmembranous