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- territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
- (mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function
- the 16th letter of the Roman alphabet (同)p
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- (国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/01/26 11:26:41」(JST)
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Phosphotyrosine-binding domain |
Structure of the PTB domain of tensin1.[1]
|
Identifiers |
Symbol |
PTB |
Pfam |
PF08416 |
InterPro |
IPR013625 |
CDD |
cd00934 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
PTB domain (IRS-1 type) |
irs-1 ptb domain complexed with a il-4 receptor phosphopeptide, nmr, minimized average structure
|
Identifiers |
Symbol |
IRS |
Pfam |
PF02174 |
InterPro |
IPR002404 |
SMART |
PTBI |
SCOP |
1cli |
SUPERFAMILY |
1cli |
CDD |
cd01204 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
In molecular biology, Phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine.
The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (Pfam PF00017) domain and a region similar to the tumour suppressor PTEN.[2] The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.[3]
The phosphotyrosine-binding domain of insulin receptor substrate-1 is not related to the phosphotyrosine-binding domain of tensin. Insulin receptor substrate-1 proteins contain both a pleckstrin homology domain and a phosphotyrosine binding (PTB) domain. The PTB domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. The PTB domain is situated towards the N terminus. Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac-LYASSNPApY-NH2 peptide in the juxtamembrane region of the insulin receptor. Further interactions via "bridged" water molecules are coordinated by residues an Asn and a Ser residue.[4] The PTB domain has a compact, 7-stranded beta-sandwich structure, capped by a C-terminal helix. The substrate peptide fits into an L-shaped surface cleft formed from the C-terminal helix and strands 5 and 6.[5]
Human proteins containing these domains
APBA1; APBA2; APBA3; EPS8; EPS8L1; EPS8L2; EPS8L3; TENC1; TNS; TNS1; TNS3; TNS4; DOK1; DOK2; DOK3; DOK4; DOK5; DOK6; DOK7; FRS2; FRS3; IRS1; IRS2; IRS4; TLN1; TLN2
References
- ^ McCleverty CJ, Lin DC, Liddington RC (June 2007). "Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions". Protein Sci. 16 (6): 1223–9. doi:10.1110/ps.072798707. PMC 2206669. PMID 17473008.
- ^ Chen H, Ishii A, Wong WK, Chen LB, Lo SH (October 2000). "Molecular characterization of human tensin". Biochem. J. 351 (2): 403–11. doi:10.1042/0264-6021:3510403. PMC 1221376. PMID 11023826.
- ^ Lo SH (January 2004). "Tensin". Int. J. Biochem. Cell Biol. 36 (1): 31–4. doi:10.1016/S1357-2725(03)00171-7. PMID 14592531.
- ^ Eck MJ, Dhe-Paganon S, Trub T, Nolte RT, Shoelson SE (May 1996). "Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor". Cell 85 (5): 695–705. doi:10.1016/S0092-8674(00)81236-2. PMID 8646778.
- ^ Zhou MM, Huang B, Olejniczak ET, Meadows RP, Shuker SB, Miyazaki M, Trub T, Shoelson SE, Fesik SW (April 1996). "Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain". Nat. Struct. Biol. 3 (4): 388–93. doi:10.1038/nsb0496-388. PMID 8599766.
External links
- Eukaryotic Linear Motif resource motif class LIG_PTB_Phospho_1
This article incorporates text from the public domain Pfam and InterPro IPR013625
This article incorporates text from the public domain Pfam and InterPro IPR002404
UpToDate Contents
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English Journal
- Examining the Effect of the Dipole Moment on Charge Separation in Donor-Acceptor Polymers for Organic Photovoltaic Applications.
- Carsten B, Szarko JM, Son HJ, Wang W, Lu L, He F, Rolczynski BS, Lou SJ, Chen LX, Yu L.SourceDepartment of Chemistry and the James Franck Institute, The University of Chicago , 929 East 57th Street, Chicago, Illinois 60637, United States.
- Journal of the American Chemical Society.J Am Chem Soc.2011 Nov 22. [Epub ahead of print]
- A new low band gap copolymer PBB3 containing [6,6']bi[thieno[3,4-b]thiophenyl]-2,2'-dicarboxylic acid bis-(2-butyloctyl) ester (BTT) and 4,8-bis(2-butyloctyl)benzo[1,2-b:4,5-b']dithiophene (BDT) units was synthesized and tested for solar cell efficiency. PBB3 showed a broad absorbance in the near-IR
- PMID 22077184
- Adaptor protein containing PH domain, PTB domain and leucine zipper (APPL1) regulates the protein level of EGFR by modulating its trafficking.
- Lee JR, Hahn HS, Kim YH, Nguyen HH, Yang JM, Kang JS, Hahn MJ.SourceDepartment of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Republic of Korea.
- Biochemical and biophysical research communications.Biochem Biophys Res Commun.2011 Nov 11;415(1):206-11. Epub 2011 Oct 19.
- The EGFR-mediated signaling pathway regulates multiple biological processes such as cell proliferation, survival and differentiation. Previously APPL1 (adaptor protein containing PH domain, PTB domain and leucine zipper 1) has been reported to function as a downstream effector of EGF-initiated signa
- PMID 22037462
Japanese Journal
- 25pTB-10 テラヘルツ分光法により観測される広範囲におよぶリン脂質二重膜の水和状態(25pTB 複雑液体(エマルジョン・膜・コロイド),領域12(ソフトマター物理,化学物理,生物物理))
- Role of IRS and PHIP on insulin-induced tyrosine phosphorylation and distribution of IRS proteins
- Kaburagi Yasushi,Okochi Hitoshi,Satoh Shinobu [他]
- Cell Structure and Function 32(1・2), 69-78, 2007-12
- NAID 40016192020
Related Links
- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】リン酸化チロシン(Phospho/Tyr)結合: PTB ドメイン(領域)ページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
- PDB code Main view Title 1aqc X11 PTB DOMAIN-10MER PEPTIDE COMPLEX 1ddm SOLUTION STRUCTURE OF THE NUMB PTB DOMAIN COMPLEXED TO A NAK PEPTIDE 1m7e Crystal structure of the phosphotyrosine ...
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