Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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V.Leong,
J.Lorenowicz,
N.Kozij,
and
A.Guarné
(2009).
Nuclear import of human MLH1, PMS2, and MutLalpha: redundancy is the key.
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Mol Carcinog, 48,
742-750.
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W.Sjursen,
I.Bjørnevoll,
L.F.Engebretsen,
K.Fjelland,
T.Halvorsen,
and
H.E.Myrvold
(2009).
A homozygote splice site PMS2 mutation as cause of Turcot syndrome gives rise to two different abnormal transcripts.
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Fam Cancer, 8,
179-186.
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I.Marinovic-Terzic,
A.Yoshioka-Yamashita,
H.Shimodaira,
E.Avdievich,
I.C.Hunton,
R.D.Kolodner,
W.Edelmann,
and
J.Y.Wang
(2008).
Apoptotic function of human PMS2 compromised by the nonsynonymous single-nucleotide polymorphic variant R20Q.
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Proc Natl Acad Sci U S A, 105,
13993-13998.
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K.Fukui,
M.Nishida,
N.Nakagawa,
R.Masui,
and
S.Kuramitsu
(2008).
Bound nucleotide controls the endonuclease activity of mismatch repair enzyme MutL.
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J Biol Chem, 283,
12136-12145.
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S.Krüger,
M.Kinzel,
C.Walldorf,
S.Gottschling,
A.Bier,
S.Tinschert,
A.von Stackelberg,
W.Henn,
H.Görgens,
S.Boue,
K.Kölble,
R.Büttner,
and
H.K.Schackert
(2008).
Homozygous PMS2 germline mutations in two families with early-onset haematological malignancy, brain tumours, HNPCC-associated tumours, and signs of neurofibromatosis type 1.
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Eur J Hum Genet, 16,
62-72.
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D.G.Shpakovskii,
E.K.Shematorova,
and
G.V.Shpakovskii
(2006).
Human PMS2 gene family: origin, molecular evolution, and biological implications.
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Dokl Biochem Biophys, 408,
175-179.
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F.J.López de Saro,
M.G.Marinus,
P.Modrich,
and
M.O'Donnell
(2006).
The beta sliding clamp binds to multiple sites within MutL and MutS.
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J Biol Chem, 281,
14340-14349.
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G.Plotz,
C.Welsch,
L.Giron-Monzon,
P.Friedhoff,
M.Albrecht,
A.Piiper,
R.M.Biondi,
T.Lengauer,
S.Zeuzem,
and
J.Raedle
(2006).
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
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Nucleic Acids Res, 34,
6574-6586.
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G.Plotz,
S.Zeuzem,
and
J.Raedle
(2006).
DNA mismatch repair and Lynch syndrome.
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J Mol Histol, 37,
271-283.
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M.Clendenning,
H.Hampel,
J.LaJeunesse,
A.Lindblom,
J.Lockman,
M.Nilbert,
L.Senter,
K.Sotamaa,
and
A.de la Chapelle
(2006).
Long-range PCR facilitates the identification of PMS2-specific mutations.
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Hum Mutat, 27,
490-495.
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S.H.Jun,
T.G.Kim,
and
C.Ban
(2006).
DNA mismatch repair system. Classical and fresh roles.
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FEBS J, 273,
1609-1619.
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T.A.Kunkel,
and
D.A.Erie
(2005).
DNA mismatch repair.
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Annu Rev Biochem, 74,
681-710.
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S.M.Lipkin,
L.S.Rozek,
G.Rennert,
W.Yang,
P.C.Chen,
J.Hacia,
N.Hunt,
B.Shin,
S.Fodor,
M.Kokoris,
J.K.Greenson,
E.Fearon,
H.Lynch,
F.Collins,
and
S.B.Gruber
(2004).
The MLH1 D132H variant is associated with susceptibility to sporadic colorectal cancer.
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Nat Genet, 36,
694-699.
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C.E.Schrader,
J.Vardo,
and
J.Stavnezer
(2003).
Mlh1 can function in antibody class switch recombination independently of Msh2.
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J Exp Med, 197,
1377-1383.
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E.Antony,
and
M.M.Hingorani
(2003).
Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair.
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Biochemistry, 42,
7682-7693.
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E.R.Hoffmann,
P.V.Shcherbakova,
T.A.Kunkel,
and
R.H.Borts
(2003).
MLH1 mutations differentially affect meiotic functions in Saccharomyces cerevisiae.
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Genetics, 163,
515-526.
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M.C.Hall,
P.V.Shcherbakova,
J.M.Fortune,
C.H.Borchers,
J.M.Dial,
K.B.Tomer,
and
T.A.Kunkel
(2003).
DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair.
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Nucleic Acids Res, 31,
2025-2034.
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M.J.Schofield,
and
P.Hsieh
(2003).
DNA mismatch repair: molecular mechanisms and biological function.
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Annu Rev Microbiol, 57,
579-608.
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P.Chène
(2003).
The ATPases: a new family for a family-based drug design approach.
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Expert Opin Ther Targets, 7,
453-461.
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B.A.Owen,
W.P.Sullivan,
S.J.Felts,
and
D.O.Toft
(2002).
Regulation of heat shock protein 90 ATPase activity by sequences in the carboxyl terminus.
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J Biol Chem, 277,
7086-7091.
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C.Welz-Voegele,
J.E.Stone,
P.T.Tran,
H.M.Kearney,
R.M.Liskay,
T.D.Petes,
and
S.Jinks-Robertson
(2002).
Alleles of the yeast Pms1 mismatch-repair gene that differentially affect recombination- and replication-related processes.
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Genetics, 162,
1131-1145.
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G.Tomer,
A.B.Buermeyer,
M.M.Nguyen,
and
R.M.Liskay
(2002).
Contribution of human mlh1 and pms2 ATPase activities to DNA mismatch repair.
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J Biol Chem, 277,
21801-21809.
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M.C.Hall,
P.V.Shcherbakova,
and
T.A.Kunkel
(2002).
Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins.
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J Biol Chem, 277,
3673-3679.
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M.Räschle,
P.Dufner,
G.Marra,
and
J.Jiricny
(2002).
Mutations within the hMLH1 and hPMS2 subunits of the human MutLalpha mismatch repair factor affect its ATPase activity, but not its ability to interact with hMutSalpha.
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J Biol Chem, 277,
21810-21820.
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P.Chène
(2002).
ATPases as drug targets: learning from their structure.
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Nat Rev Drug Discov, 1,
665-673.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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321 a.a.
302 a.a.
-strands are shown as purple arrows,
and 3[10] helices as gold ribbons and connecting loops as light green coils. Disordered loops are shown as green dotted lines. Secondary structures are labeled using the same convention as for the LN40 structure. New structural elements in NhPMS2 are labeled with the same name as the following structural element with a prime (E' helix lies between D and E helices). N- and C-termini are marked for clarity. (C) Sequence alignment of hPMS2, hMLH1 and MutL. Loops undergoing structural transformation in LN40 are labeled and shown in orange. ATP binding motifs (I -IV) are boxed in blue. The residues conserved in the GHL superfamily are shaded in blue, the rest of the conserved residues are shaded in light yellow.
S (E). The ATP lids are shown in solid magenta when traceable. The start and end residues of the ATP lid of NhPMS2 structures are labeled and marked with red and blue arrowheads, respectively. Side chains of conserved residues involved in nucleotide binding are shown as ball-and-sticks. Arg95 of LN40 and its equivalent, Arg107 of hPMS2, are shown as magenta ball-and-sticks. The bound nucleotide is shown as a gray stick model.
