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词条 Protein dimer
释义

  1. Examples

  2. See also

  3. References

In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word dimer has roots meaning "two parts", di- + -mer. A protein dimer is a type of protein quaternary structure.

A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins.

Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains.[1] An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO.[2]

Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity.[3]

Examples

  • Antibodies
  • Receptor tyrosine kinases
  • Transcription factors
    • Leucine zipper motif proteins
    • Nuclear receptors
  • 14-3-3 proteins
  • G protein-coupled receptors
  • G protein βγ-subunit dimer
  • Kinesin
  • Triosephosphateisomerase (TIM)
  • Alcohol dehydrogenase
  • Factor XI
  • Factor XIII
  • Toll-like receptor
  • Fibrinogen
  • Variable surface glycoproteins of the Trypanosoma parasite
  • Tubulin
  • Type II restriction enzymes

See also

  • Dimer (chemistry)
  • Protein trimer
  • Oligomer
  • ProtCID

References

1. ^{{cite journal |vauthors=Sluis-Cremer N, Hamamouch N, San Félix A, Velazquez S, Balzarini J, Camarasa MJ | title = Structure-activity relationships of [2',5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]- 3'-spiro-5' '-(4' '-amino-1' ',2' '-oxathiole-2' ',2' '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization | journal = J. Med. Chem. | volume = 49 | issue = 16 | pages = 4834–41 |date=August 2006 | pmid = 16884295 | doi = 10.1021/jm0604575 }}
2. ^{{cite journal |vauthors=Herscovitch M, Comb W, Ennis T, Coleman K, Yong S, Armstead B, Kalaitzidis D, Chandani S, Gilmore TD | title = Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347 | journal = Biochemical and Biophysical Research Communications | volume = 367 | issue = 1 | pages = 103–8 |date=February 2008 | pmid = 18164680 | pmc = 2277332 | doi = 10.1016/j.bbrc.2007.12.123 | url = }}
3. ^{{Cite journal|last=Amoutzias|first=Grigoris D.|last2=Robertson|first2=David L.|last3=Van de Peer|first3=Yves|last4=Oliver|first4=Stephen G.|date=2008-05-01|title=Choose your partners: dimerization in eukaryotic transcription factors|journal=Trends in Biochemical Sciences|volume=33|issue=5|pages=220–229|doi=10.1016/j.tibs.2008.02.002|issn=0968-0004|pmid=18406148}}
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2 : Protein structure|Dimers (chemistry)

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