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TitlePMS2 variant results in loss of ATPase activity without compromising mismatch repair.
Journal, issue, pagesMol Genet Genomic Med, Vol. 10, Page e1908-e1908, Year 2022
Publish dateJul 7, 2021 (structure data deposition date)
AuthorsD'Arcy, B.M. / Arrington, J. / Weisman, J. / McClellan, S.B. / Yang, Z. / Deivanayagam, C. / Blount, J. / Prakash, A.
External linksMol Genet Genomic Med / PubMed:35189042
MethodsX-ray diffraction
Resolution2 - 2.12 Å
Structure data

PDB-7rcb:
Crystal Structure of a PMS2 VUS
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-7rci:
Crystal Structure of a PMS2 VUS with Substrate
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

PDB-7rck:
Crystal Structure of PMS2 with Substrate
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Mismatch Repair / Variant of Uncertain Significance / ATPase Domain / DNA Repair Enzyme

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