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The CBS Domain: A Protein Module with an Emerging Prominent Role in Regulation
Tekijät: Baykov AA, Tuominen HK, Lahti R
Kustantaja: AMER CHEMICAL SOC
Julkaisuvuosi: 2011
Journal: ACS Chemical Biology
Tietokannassa oleva lehden nimi: ACS CHEMICAL BIOLOGY
Lehden akronyymi: ACS CHEM BIOL
Numero sarjassa: 11
Vuosikerta: 6
Numero: 11
Aloitussivu: 1156
Lopetussivu: 1163
Sivujen määrä: 8
ISSN: 1554-8929
DOI: https://doi.org/10.1021/cb200231c
Tiivistelmä
Regulatory CBS (cystathionine beta-synthase) domains exist as two or four tandem copies in thousands of cytosolic and membrane-associated proteins from all kingdoms of life Mutations in the CBS domains of human enzymes and membrane channels are associated with an array of hereditary diseases. Four CBS domains encoded within a single polypeptide or two identical polypeptidess (each having a pair of CBS domains at the subunit interface) form a highly conserved disk like structure. CBS domains act as autoinhibitory regulatory units in some proteins and activate or further inhibit protein function upon binding to adenosine nucleotides (AMP, ADP, ATP, S-adenosyl methionine, NAD, diadenosine polyphosphates). As a result of the differential effects of the nucleotides, CBS domain-containing proteins can sense cell energy levels. Significant conformational changes are induced in CBS domains by bound ligands, highlighting the structural basis for their effects.
Regulatory CBS (cystathionine beta-synthase) domains exist as two or four tandem copies in thousands of cytosolic and membrane-associated proteins from all kingdoms of life Mutations in the CBS domains of human enzymes and membrane channels are associated with an array of hereditary diseases. Four CBS domains encoded within a single polypeptide or two identical polypeptidess (each having a pair of CBS domains at the subunit interface) form a highly conserved disk like structure. CBS domains act as autoinhibitory regulatory units in some proteins and activate or further inhibit protein function upon binding to adenosine nucleotides (AMP, ADP, ATP, S-adenosyl methionine, NAD, diadenosine polyphosphates). As a result of the differential effects of the nucleotides, CBS domain-containing proteins can sense cell energy levels. Significant conformational changes are induced in CBS domains by bound ligands, highlighting the structural basis for their effects.
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