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PDBsum entry 1a1x
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Proto-oncogene PDB id
1a1x

 

 

 

 

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Contents
Protein chain
106 a.a. *
Waters ×24
* Residue conservation analysis
PDB id:
1a1x
Name: Proto-oncogene
Title: Crystal structure of mtcp-1 involved in t cell malignancies
Structure: Hmtcp-1. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.00Å     R-factor:   0.211     R-free:   0.253
Authors: Z.Q.Fu,G.C.Dubois,S.P.Song,I.Kulikovskaya,L.Virgilio,J.Rothstein, C.M.Croce,I.T.Weber,R.W.Harrison
Key ref:
Z.Q.Fu et al. (1998). Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies. Proc Natl Acad Sci U S A, 95, 3413-3418. PubMed id: 9520380 DOI: 10.1073/pnas.95.7.3413
Date:
18-Dec-97     Release date:   27-May-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56278  (MTCP1_HUMAN) -  Protein p13 MTCP-1 from Homo sapiens
Seq:
Struc: 		107 a.a.
106 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1073/pnas.95.7.3413 Proc Natl Acad Sci U S A 95:3413-3418 (1998)
PubMed id: 9520380  
 
 
Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies.
Z.Q.Fu, G.C.Du Bois, S.P.Song, I.Kulikovskaya, L.Virgilio, J.L.Rothstein, C.M.Croce, I.T.Weber, R.W.Harrison.
 
  ABSTRACT  
 
Two related oncogenes, TCL-1 and MTCP-1, are overexpressed in T cell prolymphocytic leukemias as a result of chromosomal rearrangements that involve the translocation of one T cell receptor gene to either chromosome 14q32 or Xq28. The crystal structure of human recombinant MTCP-1 protein has been determined at 2.0 A resolution by using multiwavelength anomalous dispersion data from selenomethionine-enriched protein and refined to an R factor of 0.21. MTCP-1 folds into a compact eight-stranded beta barrel structure with a short helix between the fourth and fifth strands. The topology is unique. The structure of TCL-1 has been predicted by molecular modeling based on 40% amino acid sequence identity with MTCP-1. The identical residues are clustered inside the barrel and on the surface at one side of the barrel. The overall structure of MTCP-1 superficially resembles the structures of proteins in the lipocalin family and calycin superfamily. These proteins have diverse functions, including transport of retinol, fatty acids, chromophores, pheromones, synthesis of prostaglandin, immune modulation, and cell regulation. However, MTCP-1 differs in the topology of the beta strands. The structural similarity suggests that MTCP-1 and TCL-1 form a unique family of beta barrel proteins that is predicted to bind small hydrophobic ligands and function in cell regulation.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Crystal structure of MTCP-1. A MOLSCRIPT (36) ribbon representation with arrows indicating strands. Two orthogonal views are shown in A and B. 		Figure 3.
Fig. 3. (A) Topology of the eight-stranded antiparallel barrel of MTCP-1. strands A to H are indicated by arrows and the helix by a cylinder. (B) Topology of the lipocalin fold. The strands A to H are indicated by arrows, the helix by a cylinder, and the amino-terminal 3[10] helix by an ellipse.
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17890451 M.Herling, K.A.Patel, M.A.Teitell, M.Konopleva, F.Ravandi, R.Kobayashi, and D.Jones (2008).
High TCL1 expression and intact T-cell receptor signaling define a hyperproliferative subset of T-cell prolymphocytic leukemia.
  Blood, 111, 328-337.  
16131749 B.Heras, and J.L.Martin (2005).
Post-crystallization treatments for improving diffraction quality of protein crystals.
  Acta Crystallogr D Biol Crystallogr, 61, 1173-1180.  
16056259 M.A.Teitell (2005).
The TCL1 family of oncoproteins: co-activators of transformation.
  Nat Rev Cancer, 5, 640-648.  
15621749 I.Munk Pedersen, and J.Reed (2004).
Microenvironmental interactions and survival of CLL B-cells.
  Leuk Lymphoma, 45, 2365-2372.  
12181493 M.G.Narducci, M.T.Fiorenza, S.M.Kang, A.Bevilacqua, M.Di Giacomo, D.Remotti, M.C.Picchio, V.Fidanza, M.D.Cooper, C.M.Croce, F.Mangia, and G.Russo (2002).
TCL1 participates in early embryonic development and is overexpressed in human seminomas.
  Proc Natl Acad Sci U S A, 99, 11712-11717.  
11679718 J.M.Petock, I.Y.Torshin, Y.F.Wang, G.C.Du Bois, C.M.Croce, R.W.Harrison, and I.T.Weber (2001).
Structure of murine Tcl1 at 2.5 A resolution and implications for the TCL oncogene family.
  Acta Crystallogr D Biol Crystallogr, 57, 1545-1551.
PDB code: 1jnp
11320330 J.M.Petock, Y.F.Wang, G.C.DuBois, R.W.Harrison, and I.T.Weber (2001).
Effects of different post-crystallization soaking conditions on the diffraction of Mtcp1 crystals.
  Acta Crystallogr D Biol Crystallogr, 57, 763-765.  
11058743 D.R.Flower, A.C.North, and C.E.Sansom (2000).
The lipocalin protein family: structural and sequence overview.
  Biochim Biophys Acta, 1482, 9.  
10716693 Y.Pekarsky, A.Koval, C.Hallas, R.Bichi, M.Tresini, S.Malstrom, G.Russo, P.Tsichlis, and C.M.Croce (2000).
Tcl1 enhances Akt kinase activity and mediates its nuclear translocation.
  Proc Natl Acad Sci U S A, 97, 3028-3033.  
10588720 C.Hallas, Y.Pekarsky, T.Itoyama, J.Varnum, R.Bichi, J.L.Rothstein, and C.M.Croce (1999).
Genomic analysis of human and mouse TCL1 loci reveals a complex of tightly clustered genes.
  Proc Natl Acad Sci U S A, 96, 14418-14423.  
10360182 G.C.Paesen, P.L.Adams, K.Harlos, P.A.Nuttall, and D.I.Stuart (1999).
Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure.
  Mol Cell, 3, 661-671.
PDB codes: 1qft 1qfv
10077617 Y.Pekarsky, C.Hallas, M.Isobe, G.Russo, and C.M.Croce (1999).
Abnormalities at 14q32.1 in T cell malignancies involve two oncogenes.
  Proc Natl Acad Sci U S A, 96, 2949-2951.  
10089389 Z.Q.Fu, G.C.Du Bois, S.P.Song, R.W.Harrison, and I.T.Weber (1999).
Improving the diffraction quality of MTCP-1 crystals by post-crystallization soaking.
  Acta Crystallogr D Biol Crystallogr, 55, 5-7.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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