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PDBsum entry 1a1x
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Proto-oncogene
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PDB id
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1a1x
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References listed in PDB file
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Key reference
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Title
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Crystal structure of mtcp-1: implications for role of tcl-1 and mtcp-1 in t cell malignancies.
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Authors
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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.
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Ref.
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Proc Natl Acad Sci U S A, 1998,
95,
3413-3418.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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