1HP8

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

Summary for 1HP8

• Entry DOI: 10.2210/pdb1hp8/pdb
• Descriptor: Cx9C motif-containing protein 4 (1 entity in total)
• Functional Keywords: hu-p8, leukemia, cysteine motif
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 8889.19

Authors

Barthe, P.,Chiche, L.,Strub, M.P.,Roumestand, C. (deposition date: 1997-08-26, release date: 1998-03-04, Last modification date: 2024-11-20)

Primary citation

Barthe, P.,Yang, Y.S.,Chiche, L.,Hoh, F.,Strub, M.P.,Guignard, L.,Soulier, J.,Stern, M.H.,van Tilbeurgh, H.,Lhoste, J.M.,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., 274:801-815, 1997

PubMed Abstract: 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.

PubMed: 9405159
DOI: 10.1006/jmbi.1997.1438

Experimental method

SOLUTION NMR