Human programmed cell death 5 protein has a helical-core and two dissociated structural regions

被引:24
作者
Liu, DS [1 ]
Feng, YG [1 ]
Cheng, Y [1 ]
Wang, JF [1 ]
机构
[1] Acad Sinica, Inst Biophys, Ctr Mol Biol, Natl Lab Biomacromol, Beijing 100101, Peoples R China
基金
中国国家自然科学基金;
关键词
programmed cell death 5; heteronuclear NMR method; triple-helix bundle; dynamic behavior;
D O I
10.1016/j.bbrc.2004.04.044
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Programmed cell death 5 (PDCD5) protein is phylogenetically conserved in both the nucleus and cytoplasm. The human PDCD5 protein is expressed in tumor cells during apoptosis independent of the apoptosis-inducing stimuli, and recently it was found that PDCD5 is an important regulator in both apoptotic and non-apoptotic programmed cell death. In this study, human PDCD5 was expressed in Escherichia coli cell and studied using heteronuclear NMR method. The NMR results indicate that PDCD5 protein call be divided into three Structural re-ions, a core region and two dissociated terminal re ions. The core region (41-101) represents a rigid sub-domain consisting mainly of a triple-helix bundle. The N-terminal 38 residues (3-40) are ordered, but not a rigid Structural region which contains abundant secondary structure, and packs very loosely against the core. The C-terminal 17 residues ( 102-118) represent a mobile unstructured region. which may be capable of interaction with nucleic acid. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:391 / 396
页数:6
相关论文
共 19 条
[1]
[Anonymous], 2018, Protein nmr spectroscopy: principles and practice
[2]
Shape space from deformation [J].
Cheng, HL ;
Edelsbrunner, H ;
Fu, P .
COMPUTATIONAL GEOMETRY-THEORY AND APPLICATIONS, 2001, 19 (2-3) :191-204
[3]
An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation [J].
Cheng, Y ;
Liu, DS ;
Feng, YM ;
Jing, GZ .
PROTEIN AND PEPTIDE LETTERS, 2003, 10 (02) :175-181
[4]
Christendat D, 2000, NAT STRUCT BIOL, V7, P903
[5]
BACKBONE DYNAMICS OF A FREE AND A PHOSPHOPEPTIDE-COMPLEXED SRC HOMOLOGY-2 DOMAIN STUDIED BY N-15 NMR RELAXATION [J].
FARROW, NA ;
MUHANDIRAM, R ;
SINGER, AU ;
PASCAL, SM ;
KAY, CM ;
GISH, G ;
SHOELSON, SE ;
PAWSON, T ;
FORMANKAY, JD ;
KAY, LE .
BIOCHEMISTRY, 1994, 33 (19) :5984-6003
[6]
FILATOV D, 1992, J BIOL CHEM, V267, P15816
[7]
ESPript:: analysis of multiple sequence alignments in PostScript [J].
Gouet, P ;
Courcelle, E ;
Stuart, DI ;
Métoz, F .
BIOINFORMATICS, 1999, 15 (04) :305-308
[8]
Protein-RNA interactions: a structural analysis [J].
Jones, S ;
Daley, DTA ;
Luscombe, NM ;
Berman, HM ;
Thornton, JM .
NUCLEIC ACIDS RESEARCH, 2001, 29 (04) :943-954
[9]
A SIMPLE METHOD FOR DISPLAYING THE HYDROPATHIC CHARACTER OF A PROTEIN [J].
KYTE, J ;
DOOLITTLE, RF .
JOURNAL OF MOLECULAR BIOLOGY, 1982, 157 (01) :105-132
[10]
CHARACTERIZATION OF A FUNCTIONALLY IMPORTANT MOBILE DOMAIN OF GROES [J].
LANDRY, SJ ;
ZEILSTRARYALLS, J ;
FAYET, O ;
GEORGOPOULOS, C ;
GIERASCH, LM .
NATURE, 1993, 364 (6434) :255-258