SOLUTION STRUCTURE OF HUMAN P8-MTCP1, A CYSTEINE-RICH PROTEIN ENCODED BY THE MTCP1 ONCOGENE,REVEALS A NEW ALPHA-HELICAL ASSEMBLY MOTIF, NMR, 30 STRUCTURESSOLUTION STRUCTURE OF HUMAN P8-MTCP1, A CYSTEINE-RICH PROTEIN ENCODED BY THE MTCP1 ONCOGENE,REVEALS A NEW ALPHA-HELICAL ASSEMBLY MOTIF, NMR, 30 STRUCTURES

Structural highlights

2hp8 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 30 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CMC4_HUMAN Note=Overexpressed in T-cell leukemia bearing a t(X;14) translocation.

Function

CMC4_HUMAN

Publication Abstract from PubMed

MTCP1 (for Mature-T-Cell Proliferation) is the first gene unequivocally identified in the group of uncommon leukemias with a mature phenotype. The three-dimensional solution structure of the human p8(MTCP1) protein encoded by the MTCP1 oncogene was determined by homonuclear proton two-dimensional NMR methods at 600 MHz. After sequence specific assignments, a total of 931 distance restraints and 57 dihedral restraints were collected. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of p8(MTCP1) is presented as a set of 30 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol with the AMBER force field. The r.m.s.d. values with respect to the mean structure for the backbone and all heavy atoms for a family of 30 structures are 0.73(+/-0.28) and 1.17(+/-0.23) A, when the structured core of the protein (residues 5 to 63) is considered. The solution structure of p8(MTCP1) reveals an original scaffold consisting of three alpha helices, associated with a new cysteine motif. Two of the helices are covalently paired by two disulfide bridges, forming an alpha-hairpin which resembles an antiparallel coiled-coil. The third helix is oriented roughly parallel to the plane defined by the alpha-antiparallel motif and its axis forms an angle of approximately 60 degrees with respect to the main axis of this motif.

Solution structure of human p8MTCP1, a cysteine-rich protein encoded by the MTCP1 oncogene, reveals a new alpha-helical assembly motif.,Barthe P, Yang YS, Chiche L, Hoh F, Strub MP, Guignard L, Soulier J, Stern MH, van Tilbeurgh H, Lhoste JM, Roumestand C J Mol Biol. 1997 Dec 19;274(5):801-15. PMID:9405159[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Barthe P, Yang YS, Chiche L, Hoh F, Strub MP, Guignard L, Soulier J, Stern MH, van Tilbeurgh H, Lhoste JM, Roumestand C. Solution structure of human p8MTCP1, a cysteine-rich protein encoded by the MTCP1 oncogene, reveals a new alpha-helical assembly motif. J Mol Biol. 1997 Dec 19;274(5):801-15. PMID:9405159 doi:http://dx.doi.org/S0022-2836(97)91438-8
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