Solution structure of the capsid protein from the human T-cell leukemia virus type-I

被引:83
作者
Khorasanizadeh, S
Campos-Olivas, R
Summers, MF [1 ]
机构
[1] Univ Maryland Baltimore Cty, Howard Hughes Med Inst, Baltimore, MD 21250 USA
[2] Univ Maryland Baltimore Cty, Dept Biochem & Chem, Baltimore, MD 21250 USA
关键词
HTLV-I; capsid protein; retrovirus; three-dimensional structure; heteronuclear NMR spectroscopy;
D O I
10.1006/jmbi.1999.2986
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The solution structure of the capsid protein (CA) from the human T-cell leukemia virus type one (HTLV-I), a retrovirus that causes T-cell leukemia and HTLV-I-associated myelopathy in humans, has been determined by NMR methods. The protein consists of independent N and C-terminal domains connected by a flexible linker. The domains are structurally similar to the N-terminal "core" and C-terminal "dimerization" domains, respectively, of the human immunodeficiency virus type one (HIV-1) and equine infectious anemia virus (EIAV) capsid proteins, although several important differences exist. In particular, hydrophobic residues near the major homology region are partially buried in HTLV-I CA, which is monomeric in solution, whereas analogous residues in HIV-1 and EIAV CA project from the C-terminal domain and promote dimerization: These differences in the structure and oligomerization state of the proteins appear to be related to, and possibly controlled by, the oxidation state of conserved cysteine residues, which are reduced in HTLV-I CA but form a disulfide bond in the HIV-1 and EIAV CA crystal structures. The results are consistent with an oxidative capsid assembly mechanism, in which CA oligomerization or maturation is triggered by disulfide bond formation as the budding virus enters the oxidizing environment of the bloodstream. (C) 1999 Academic Press.
引用
收藏
页码:491 / 505
页数:15
相关论文
共 76 条
  • [11] STRUCTURES OF LARGER PROTEINS IN SOLUTION - 3-DIMENSIONAL AND 4-DIMENSIONAL HETERONUCLEAR NMR-SPECTROSCOPY
    CLORE, GM
    GRONENBORN, AM
    [J]. SCIENCE, 1991, 252 (5011) : 1390 - 1399
  • [12] NMRPIPE - A MULTIDIMENSIONAL SPECTRAL PROCESSING SYSTEM BASED ON UNIX PIPES
    DELAGLIO, F
    GRZESIEK, S
    VUISTER, GW
    ZHU, G
    PFEIFER, J
    BAX, A
    [J]. JOURNAL OF BIOMOLECULAR NMR, 1995, 6 (03) : 277 - 293
  • [13] FUNCTIONAL DOMAINS OF THE CAPSID PROTEIN OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1
    DORFMAN, T
    BUKOVSKY, A
    OHAGEN, A
    HOGLUND, S
    GOTTLINGER, HG
    [J]. JOURNAL OF VIROLOGY, 1994, 68 (12) : 8180 - 8187
  • [14] TISSUE SULFHYDRYL GROUPS
    ELLMAN, GL
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1959, 82 (01) : 70 - 77
  • [15] Human T-cell leukemia viruses: Epidemiology, biology, and pathogenesis
    Ferreira, OC
    Planelles, V
    Rosenblatt, JD
    [J]. BLOOD REVIEWS, 1997, 11 (02) : 91 - 104
  • [16] SPECIFICITY AND SEQUENCE REQUIREMENTS FOR INTERACTIONS BETWEEN VARIOUS RETROVIRAL GAG PROTEINS
    FRANKE, EK
    YUAN, HEH
    BOSSOLT, KL
    GOFF, SP
    LUBAN, J
    [J]. JOURNAL OF VIROLOGY, 1994, 68 (08) : 5300 - 5305
  • [17] FRANKE KE, 1994, NATURE, V24, P359
  • [18] HIV-1: Fifteen proteins and an RNA
    Frankel, AD
    Young, JAT
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1998, 67 : 1 - 25
  • [19] Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    Gamble, TR
    Vajdos, FF
    Yoo, SH
    Worthylake, DK
    Houseweart, M
    Sundquist, WI
    Hill, CP
    [J]. CELL, 1996, 87 (07) : 1285 - 1294
  • [20] Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    Gamble, TR
    Yoo, SH
    Vajdos, FF
    vonSchwedler, UK
    Worthylake, DK
    Wang, H
    McCutcheon, JP
    Sundquist, WI
    Hill, CP
    [J]. SCIENCE, 1997, 278 (5339) : 849 - 853