Allostery in membrane proteins

被引:21
作者
Cournia, Zoe [1 ]
Chatzigoulas, Alexios [1 ,2 ]
机构
[1] Acad Athens, Biomed Res Fdn, Athens 11527, Greece
[2] Natl & Kapodistrian Univ Athens, Dept Informat & Telecommun, Athens 16784, Greece
关键词
FUNCTIONAL SELECTIVITY; C2; DOMAIN; MODULATION; MECHANISM; BINDING; RECEPTOR; CHOLESTEROL; HEMOGLOBIN; INHIBITOR; BLOOD;
D O I
10.1016/j.sbi.2020.03.006
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
Membrane proteins are an integral part of signal transduction. To signal, membrane proteins must interact with a variety of lipid species, effectors, and other proteins in the biological membrane leading to an immense number of possible interactions. Despite this inherent complexity, accurate control of signaling must take place. By allowing proteins to adopt a multiplicity of conformations in a process known as allostery, nature is able to transmit a signal from one protein site to another distal, functional site, allowing for modulation of protein properties and regulation of activity. In recent years, an increasing number of reports have pointed to common mechanisms governing the allosteric modulation of membrane proteins, including conformational selection, oligomerization, and the modulation of allosteric sites. In this report, we summarize recent advances in membrane protein allostery.
引用
收藏
页码:197 / 204
页数:8
相关论文
共 61 条
  • [1] Adair GS, 1925, J BIOL CHEM, V63, P515
  • [2] KRAS Dimerization Impacts MEK Inhibitor Sensitivity and Oncogenic Activity of Mutant KRAS
    Ambrogio, Chiara
    Kohler, Jens
    Zhou, Zhi-Wei
    Wang, Haiyun
    Paranal, Raymond
    Li, Jiaqi
    Capelletti, Marzia
    Caffarra, Cristina
    Li, Shuai
    Lv, Qi
    Gondi, Sudershan
    Hunter, John C.
    Lu, Jia
    Chiarle, Roberto
    Santamaria, David
    Westover, Kenneth D.
    Janne, Pasi A.
    [J]. CELL, 2018, 172 (04) : 857 - +
  • [3] [Anonymous], 1910, J. Physiol
  • [4] α-Synuclein: Membrane Interactions and Toxicity in Parkinson's Disease
    Auluck, Pavan K.
    Caraveo, Gabriela
    Lindquist, Susan
    [J]. ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, VOL 26, 2010, 26 : 211 - 233
  • [5] Strategies for the discovery of biased GPCR ligands
    Bermudez, Marcel
    Trung Ngoc Nguyen
    Omieczynski, Christian
    Wolber, Gerhard
    [J]. DRUG DISCOVERY TODAY, 2019, 24 (04) : 1031 - 1037
  • [6] Ligand Binding Ensembles Determine Graded Agonist Efficacies at a G Protein-coupled Receptor
    Bock, Andreas
    Bermudez, Marcel
    Krebs, Fabian
    Matera, Carlo
    Chirinda, Brian
    Sydow, Dominique
    Dallanoce, Clelia
    Holzgrabe, Ulrike
    De Amici, Marco
    Lohse, Martin J.
    Wolber, Gerhard
    Mohr, Klaus
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2016, 291 (31) : 16375 - 16389
  • [7] The allosteric vestibule of a seven transmembrane helical receptor controls G-protein coupling
    Bock, Andreas
    Merten, Nicole
    Schrage, Ramona
    Dallanoce, Clelia
    Baetz, Julia
    Kloeckner, Jessica
    Schmitz, Jens
    Matera, Carlo
    Simon, Katharina
    Kebig, Anna
    Peters, Lucas
    Mueller, Anke
    Schrobang-Ley, Jasmin
    Traenkle, Christian
    Hoffmann, Carsten
    De Amici, Marco
    Holzgrabe, Ulrike
    Kostenis, Evi
    Mohr, Klaus
    [J]. NATURE COMMUNICATIONS, 2012, 3
  • [8] Bohm SK, 1997, BIOCHEM J, V322, P1
  • [9] About a new biological relation of high importance that the blood carbonic acid tension exercises on its oxygen binding.
    Bohr, C
    Hasselbalch, K
    Krogh, A
    [J]. SKANDINAVISCHES ARCHIV FUR PHYSIOLOGIE, 1904, 16 : 402 - 412
  • [10] Oligomeric Receptor Complexes and Their Allosteric Receptor-Receptor Interactions in the Plasma Membrane Represent a New Biological Principle for Integration of Signals in the CNS
    Borroto-Escuela, Dasiel O.
    Fuxe, Kjell
    [J]. FRONTIERS IN MOLECULAR NEUROSCIENCE, 2019, 12