Výsledky vyhledávání - "Lydia M. Gibson"

Variants of human thymidylate synthase with loop 181-197 stabilized in the inactive conformation

Autor: Lydia M. Gibson, Saphronia R. Johnson, Lukasz Lebioda, Leslie L. Lovelace, Sondra H. Berger, Brittnaie J. Bell

Publikováno v: Protein Science. 18:1628-1636

Loop 181-197 of human thymidylate synthase (hTS) populates two major conformations, essentially corresponding to the loop flipped by 180 degrees . In one of the conformations, the catalytic Cys195 residue lies distant from the active site making the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00cdcd6b48dafdfa6d68533008c92737
https://doi.org/10.1002/pro.171

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Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability†‡

Autor: Sondra H. Berger, Franklin G. Berger, Brittnaie J. Bell, Leslie L. Lovelace, Lukasz Lebioda, Lydia M. Gibson, Maria Marjorette O. Peña, Xiao Huang

Human and other mammalian thymidylate synthase (TS) enzymes have an N-terminal extension of approximately 27 amino acids that is not present in bacterial TSs. The extension, which is disordered in all reported crystal structures of TSs, has been cons

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b68a827a431ab4742fc4e102812d946
https://europepmc.org/articles/PMC2856444/

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Structure of the thioredoxin-like domain of yeast glutaredoxin 3

Autor: Nin N. Dingra, Caryn E. Outten, Lydia M. Gibson, Lukasz Lebioda

Yeast glutaredoxin 3 (Grx3) is a cytosolic protein that regulates the activity of the iron-responsive transcriptional activator Aft1. This member of the monothiol glutaredoxin family contains a thioredoxin-like domain and a glutaredoxin-like domain,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d120d7705e2bc817f5802e5ad7fced75
https://europepmc.org/articles/PMC2581515/

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The R163K mutant of human thymidylate synthase is stabilized in an active conformation: structural asymmetry and reactivity of cysteine 195

Autor: Lydia M. Gibson, Lukasz Lebioda, Leslie L. Lovelace

Publikováno v: Biochemistry. 47(16)

Loop 181-197 of human thymidylate synthase (hTS) populates two conformational states. In the first state, Cys195, a residue crucial for catalytic activity, is in the active site (active conformer); in the other conformation, it is about 10 A away, ou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9979fe4cd3fd0954db1fef288f06fd59
https://pubmed.ncbi.nlm.nih.gov/18370400

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Cooperative Inhibition of Human Thymidylate Synthase by Mixtures of Active Site Binding and Allosteric Inhibitors†‡

Autor: Leslie L. Lovelace, Lukasz Lebioda, Lydia M. Gibson

Thymidylate synthase (TS) is a target in the chemotherapy of colorectal cancer and some other neoplasms. It catalyzes the transfer of a methyl group from methylenetetrahydrofolate to dUMP to form dTMP. On the basis of structural considerations, we ha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4514e7ae69f7e58795d871fe13e429e
https://europepmc.org/articles/PMC2516748/

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