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PDBsum entry 1xqg
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Antitumor protein
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PDB id
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1xqg
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Contents |
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* Residue conservation analysis
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DOI no:
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J Biol Chem
279:55540-55544
(2004)
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PubMed id:
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Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained.
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M.Al-Ayyoubi,
P.G.Gettins,
K.Volz.
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ABSTRACT
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Maspin, a member of the serpin superfamily, has tumor suppressing activity
against breast and prostate cancer. Maspin inhibits tumor growth by blocking
cell invasion, and its reactive center loop (RCL) is thought to mediate this
activity. To understand this function on the molecular level, we have solved the
three-dimensional structure of Maspin to 3.1 A resolution. The molecular
structure shows the characteristic features of the serpin fold, but the RCL of
Maspin is unique in length, composition, and placement. Although the RCL of
Maspin is accessible and cleavable by some proteinases, it functions in the
uncleaved, constrained conformation observed here. These structural results will
contribute to our understanding of the mechanism by which Maspin suppresses
tumors.
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Selected figure(s)
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Figure 2.
FIG. 2. Stereo view of Maspin ribbon diagram in the typical
serpin orientation. -Strands are cyan, -helices
are magenta, and coils and turns are gold. -Sheets and helices are
labeled as in Fig. 1.
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Figure 3.
FIG. 3. Stereo diagram of the |F[o] - F[c]| omit map of
residues 330-346 of the RCL of Maspin, contoured at 2 . View
is from the back right of Fig. 2.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
55540-55544)
copyright 2004.
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Figures were
selected
by an automated process.
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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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L.C.Thompson,
S.Goswami,
D.S.Ginsberg,
D.E.Day,
I.M.Verhamme,
and
C.B.Peterson
(2011).
Metals affect the structure and activity of human plasminogen activator inhibitor-1. I. Modulation of stability and protease inhibition.
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Protein Sci,
20,
353-365.
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F.Lonardo,
X.Li,
A.Kaplun,
A.Soubani,
S.Sethi,
S.Gadgeel,
and
S.Sheng
(2010).
The natural tumor suppressor protein maspin and potential application in non small cell lung cancer.
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Curr Pharm Des,
16,
1877-1881.
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Z.S.Derewenda
(2010).
Application of protein engineering to enhance crystallizability and improve crystal properties.
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Acta Crystallogr D Biol Crystallogr,
66,
604-615.
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R.Bass,
L.Wagstaff,
L.Ravenhill,
and
V.Ellis
(2009).
Binding of extracellular maspin to beta1 integrins inhibits vascular smooth muscle cell migration.
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J Biol Chem,
284,
27712-27720.
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E.I.Chen,
and
J.R.Yates
(2006).
Maspin and tumor metastasis.
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IUBMB Life,
58,
25-29.
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A.C.Riddick,
C.J.Shukla,
C.J.Pennington,
R.Bass,
R.K.Nuttall,
A.Hogan,
K.K.Sethia,
V.Ellis,
A.T.Collins,
N.J.Maitland,
R.Y.Ball,
and
D.R.Edwards
(2005).
Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues.
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Br J Cancer,
92,
2171-2180.
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C.Benarafa,
and
E.Remold-O'Donnell
(2005).
The ovalbumin serpins revisited: perspective from the chicken genome of clade B serpin evolution in vertebrates.
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Proc Natl Acad Sci U S A,
102,
11367-11372.
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J.C.Whisstock,
S.P.Bottomley,
P.I.Bird,
R.N.Pike,
and
P.Coughlin
(2005).
Serpins 2005 - fun between the beta-sheets. Meeting report based upon presentations made at the 4th International Symposium on Serpin Structure, Function and Biology (Cairns, Australia).
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FEBS J,
272,
4868-4873.
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J.R.Birtley,
and
S.Curry
(2005).
Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal-optimization strategy.
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Acta Crystallogr D Biol Crystallogr,
61,
646-650.
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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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}
}
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