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

被引：641
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 [J].
AMATI, B ;
BROOKS, MW ;
LEVY, N ;
LITTLEWOOD, TD ;
EVAN, GI ;
LAND, H .
CELL, 1993, 72 (02) :233-245
[2]   COCRYSTALS OF THE DNA-BINDING DOMAIN OF PHAGE-434 REPRESSOR AND A SYNTHETIC PHAGE 434 OPERATOR [J].
ANDERSON, J ;
PTASHNE, M ;
HARRISON, SC .
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 [J].
ANTHONYCAHILL, SJ ;
BENFIELD, PA ;
FAIRMAN, R ;
WASSERMAN, ZR ;
BRENNER, SL ;
STAFFORD, WF ;
ALTENBACH, C ;
HUBBELL, WL ;
DEGRADO, WF .
SCIENCE, 1992, 255 (5047) :979-983
[5]   MAD - A HETERODIMERIC PARTNER FOR MAX THAT ANTAGONIZES MYC TRANSCRIPTIONAL ACTIVITY [J].
AYER, DE ;
KRETZNER, L ;
EISENMAN, RN .
CELL, 1993, 72 (02) :211-222
[6]   TFE3 - A HELIX LOOP HELIX PROTEIN THAT ACTIVATES TRANSCRIPTION THROUGH THE IMMUNOGLOBULIN ENHANCER MU-E3 MOTIF [J].
BECKMANN, H ;
SU, LK ;
KADESCH, T .
GENES & DEVELOPMENT, 1990, 4 (02) :167-179
[7]   THE PROTEIN ID - A NEGATIVE REGULATOR OF HELIX-LOOP-HELIX DNA-BINDING PROTEINS [J].
BENEZRA, R ;
DAVIS, RL ;
LOCKSHON, D ;
TURNER, DL ;
WEINTRAUB, H .
CELL, 1990, 61 (01) :49-59
[8]   FUNCTIONAL ANTAGONISM BETWEEN C-JUN AND MYOD PROTEINS - A DIRECT PHYSICAL ASSOCIATION [J].
BENGAL, E ;
RANSONE, L ;
SCHARFMANN, R ;
DWARKI, VJ ;
TAPSCOTT, SJ ;
WEINTRAUB, H ;
VERMA, IM .
CELL, 1992, 68 (03) :507-519
[9]   CASEIN KINASE-II INHIBITS THE DNA-BINDING ACTIVITY OF MAX HOMODIMERS BUT NOT MYC MAX HETERODIMERS [J].
BERBERICH, SJ ;
COLE, MD .
GENES & DEVELOPMENT, 1992, 6 (02) :166-176
[10]   PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].
BERNSTEIN, FC ;
KOETZLE, TF ;
WILLIAMS, GJB ;
MEYER, EF ;
BRICE, MD ;
RODGERS, JR ;
KENNARD, O ;
SHIMANOUCHI, T ;
TASUMI, M .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) :535-542
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