Protein trimer

Inbiochemistry,aprotein trimeris amacromolecular complexformed by three, usuallynon-covalently bound,macromoleculeslikeproteinsornucleic acids.A protein trimer often occurs from the assembly of a protein'squaternary structure.^[1]The non-covalent interactions between thehydrophobicandhydrophilicregions on thepolypeptidesunits help to stabilize the quaternary structure. Since a protein trimer is composed of multiple polypeptide subunits, it is considered anoligomer.^[2]

Ahomotrimerwould be formed by three identicalmolecules.Aheterotrimerwould be formed by three different macromolecules. Type IICollagenis an example of homotrimeric protein, while Type I collagen is an AAB-type heterotrimeric protein.

Porinsusually arrange themselves in membranes as trimers.

Bacteriophage T4 tail fiber[edit]

Multiple copies of a polypeptide encoded by ageneoften can form an aggregate referred to as a multimer.^[3]When a multimer is formed from polypeptides produced by two differentmutant allelesof a particular gene, the mixed multimer may exhibit greater functional activity than the unmixed multimers formed by each of the mutants alone. When a mixed multimer displays increased functionality relative to the unmixed multimers, the phenomenon is referred to asintragenic complementation.The distal portion of each of thebacteriophage T4tail fibers is encoded by gene37and mutants defective in this gene undergo intragenic complementation.^[4]This finding indicated that the distal tail fibers are a multimer of the gene37encoded polypeptide. An analysis of the complementation data further indicated that the polypeptides making up the multimer were folded back on themselves in the form of a hairpin. A further high-resolution crystal structure analysis of the distal tail fiber indicated that the gene37polypeptides are present as a trimer and that each polypeptide of the trimer is folded back on itself in a hairpin configuration.^[5]

References[edit]

^Godbey, W.T. (2014),"Proteins",An Introduction to Biotechnology,Elsevier, pp. 9–33,doi:10.1016/b978-1-907568-28-2.00002-2,ISBN 978-1-907568-28-2,retrieved2024-05-03
^Pelley, John W. (2012-01-01), Pelley, John W. (ed.),"3 - Protein Structure and Function",Elsevier's Integrated Review Biochemistry (Second Edition),Philadelphia: W.B. Saunders, pp. 19–28,doi:10.1016/b978-0-323-07446-9.00003-9,ISBN 978-0-323-07446-9,retrieved2024-05-03
^Crick FH, Orgel LE. The theory of inter-allelic complementation. J Mol Biol. 1964 Jan;8:161-5.doi:10.1016/s0022-2836(64)80156-x.PMID 14149958
^Bernstein H, Edgar RS, Denhardt GH. Intragenic complementation among temperature sensitive mutants of bacteriophage T4D. Genetics. 1965;51(6):987-1002.
^Bartual SG, Otero JM, Garcia-Doval C, et al. Structure of the bacteriophage T4 long tail fiber receptor-binding tip. Proc Natl Acad Sci U S A. 2010;107(47):20287-20292.doi:10.1073/pnas.1011218107

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[1] Godbey, W.T. (2014),"Proteins",An Introduction to Biotechnology,Elsevier, pp. 9–33,doi:10.1016/b978-1-907568-28-2.00002-2,ISBN 978-1-907568-28-2,retrieved2024-05-03

[2] Pelley, John W. (2012-01-01), Pelley, John W. (ed.),"3 - Protein Structure and Function",Elsevier's Integrated Review Biochemistry (Second Edition),Philadelphia: W.B. Saunders, pp. 19–28,doi:10.1016/b978-0-323-07446-9.00003-9,ISBN 978-0-323-07446-9,retrieved2024-05-03

[3] Crick FH, Orgel LE. The theory of inter-allelic complementation. J Mol Biol. 1964 Jan;8:161-5.doi:10.1016/s0022-2836(64)80156-x.PMID 14149958

[4] Bernstein H, Edgar RS, Denhardt GH. Intragenic complementation among temperature sensitive mutants of bacteriophage T4D. Genetics. 1965;51(6):987-1002.

[5] Bartual SG, Otero JM, Garcia-Doval C, et al. Structure of the bacteriophage T4 long tail fiber receptor-binding tip. Proc Natl Acad Sci U S A. 2010;107(47):20287-20292.doi:10.1073/pnas.1011218107

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Bacteriophage T4 tail fiber[edit]

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