RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN

被引：639
作者：
FERREDAMARE, AR
PRENDERGAST, GC
ZIFF, EB
BURLEY, SK
机构：
[1] ROCKEFELLER UNIV, MOLEC BIOPHYS LAB, 1230 YORK AVE, NEW YORK, NY 10021 USA
[2] ROCKEFELLER UNIV, HOWARD HUGHES MED INST LAB, NEW YORK, NY 10021 USA
[3] KAPLAN CANC CTR, DEPT BIOCHEM, NEW YORK, NY 10016 USA
[4] NYU MED CTR, HOWARD HUGHES MED INST, NEW YORK, NY 10016 USA
来源：
NATURE | 1993年 / 363卷 / 6424期
关键词：
D O I：
10.1038/363038a0
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 angstrom resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.
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页码：38 / 45
页数：8
相关论文
共 66 条
  • [1] ONCOGENIC ACTIVITY OF THE C-MYC PROTEIN REQUIRES DIMERIZATION WITH MAX
    AMATI, B
    BROOKS, MW
    LEVY, N
    LITTLEWOOD, TD
    EVAN, GI
    LAND, H
    [J]. CELL, 1993, 72 (02) : 233 - 245
  • [2] COCRYSTALS OF THE DNA-BINDING DOMAIN OF PHAGE-434 REPRESSOR AND A SYNTHETIC PHAGE 434 OPERATOR
    ANDERSON, J
    PTASHNE, M
    HARRISON, SC
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (05): : 1307 - 1311
  • [3] [Anonymous], 1989, EMBO J, V8, P1
  • [4] MOLECULAR CHARACTERIZATION OF HELIX-LOOP-HELIX PEPTIDES
    ANTHONYCAHILL, SJ
    BENFIELD, PA
    FAIRMAN, R
    WASSERMAN, ZR
    BRENNER, SL
    STAFFORD, WF
    ALTENBACH, C
    HUBBELL, WL
    DEGRADO, WF
    [J]. SCIENCE, 1992, 255 (5047) : 979 - 983
  • [5] MAD - A HETERODIMERIC PARTNER FOR MAX THAT ANTAGONIZES MYC TRANSCRIPTIONAL ACTIVITY
    AYER, DE
    KRETZNER, L
    EISENMAN, RN
    [J]. CELL, 1993, 72 (02) : 211 - 222
  • [6] TFE3 - A HELIX LOOP HELIX PROTEIN THAT ACTIVATES TRANSCRIPTION THROUGH THE IMMUNOGLOBULIN ENHANCER MU-E3 MOTIF
    BECKMANN, H
    SU, LK
    KADESCH, T
    [J]. GENES & DEVELOPMENT, 1990, 4 (02) : 167 - 179
  • [7] THE PROTEIN ID - A NEGATIVE REGULATOR OF HELIX-LOOP-HELIX DNA-BINDING PROTEINS
    BENEZRA, R
    DAVIS, RL
    LOCKSHON, D
    TURNER, DL
    WEINTRAUB, H
    [J]. CELL, 1990, 61 (01) : 49 - 59
  • [8] FUNCTIONAL ANTAGONISM BETWEEN C-JUN AND MYOD PROTEINS - A DIRECT PHYSICAL ASSOCIATION
    BENGAL, E
    RANSONE, L
    SCHARFMANN, R
    DWARKI, VJ
    TAPSCOTT, SJ
    WEINTRAUB, H
    VERMA, IM
    [J]. CELL, 1992, 68 (03) : 507 - 519
  • [9] CASEIN KINASE-II INHIBITS THE DNA-BINDING ACTIVITY OF MAX HOMODIMERS BUT NOT MYC MAX HETERODIMERS
    BERBERICH, SJ
    COLE, MD
    [J]. GENES & DEVELOPMENT, 1992, 6 (02) : 166 - 176
  • [10] PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES
    BERNSTEIN, FC
    KOETZLE, TF
    WILLIAMS, GJB
    MEYER, EF
    BRICE, MD
    RODGERS, JR
    KENNARD, O
    SHIMANOUCHI, T
    TASUMI, M
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) : 535 - 542
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