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PDBsum entry 1xqg

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protein Protein-protein interface(s) links
Antitumor protein PDB id
1xqg

 

 

 

 

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Contents
Protein chain
378 a.a. *
Waters ×152
* Residue conservation analysis
PDB id:
1xqg
Name: Antitumor protein
Title: 3.10 a crystal structure of maspin, space group p 4 21 2
Structure: Maspin. Chain: a, b. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: serpinb5, pi5. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.10Å     R-factor:   0.194     R-free:   0.252
Authors: M.Al-Ayyoubi,P.G.Gettins,K.Volz
Key ref:
M.Al-Ayyoubi et al. (2004). Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained. J Biol Chem, 279, 55540-55544. PubMed id: 15501821 DOI: 10.1074/jbc.M409957200
Date:
12-Oct-04     Release date:   26-Oct-04    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P36952  (SPB5_HUMAN) -  Serpin B5 from Homo sapiens
Seq:
Struc:
375 a.a.
378 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 

 
DOI no: 10.1074/jbc.M409957200 J Biol Chem 279:55540-55544 (2004)
PubMed id: 15501821  
 
 
Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained.
M.Al-Ayyoubi, P.G.Gettins, K.Volz.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
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.
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.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 55540-55544) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21280127 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.
  Protein Sci, 20, 353-365.  
20337574 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.
  Curr Pharm Des, 16, 1877-1881.  
20445236 Z.S.Derewenda (2010).
Application of protein engineering to enhance crystallizability and improve crystal properties.
  Acta Crystallogr D Biol Crystallogr, 66, 604-615.  
19638634 R.Bass, L.Wagstaff, L.Ravenhill, and V.Ellis (2009).
Binding of extracellular maspin to beta1 integrins inhibits vascular smooth muscle cell migration.
  J Biol Chem, 284, 27712-27720.  
16540429 E.I.Chen, and J.R.Yates (2006).
Maspin and tumor metastasis.
  IUBMB Life, 58, 25-29.  
15928670 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.
  Br J Cancer, 92, 2171-2180.  
16055559 C.Benarafa, and E.Remold-O'Donnell (2005).
The ovalbumin serpins revisited: perspective from the chicken genome of clade B serpin evolution in vertebrates.
  Proc Natl Acad Sci U S A, 102, 11367-11372.  
16176261 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).
  FEBS J, 272, 4868-4873.  
15858279 J.R.Birtley, and S.Curry (2005).
Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal-optimization strategy.
  Acta Crystallogr D Biol Crystallogr, 61, 646-650.  
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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