• HOME
  • NEWS
    • BIOENGINEERING
    • SCIENCE NEWS
  • EXPLORE
    • CAREER
      • Companies
      • Jobs
    • EVENTS
    • iGEM
      • News
      • Team
    • PHOTOS
    • VIDEO
    • WIKI
  • BLOG
  • COMMUNITY
    • FACEBOOK
    • FORUM
    • INSTAGRAM
    • TWITTER
  • CONTACT US
Friday, January 22, 2021
BIOENGINEER.ORG
No Result
View All Result
  • Login
  • HOME
  • NEWS
    • BIOENGINEERING
    • SCIENCE NEWS
  • EXPLORE
    • CAREER
      • Companies
      • Jobs
        • Lecturer
        • PhD Studentship
        • Postdoc
        • Research Assistant
    • EVENTS
    • iGEM
      • News
      • Team
    • PHOTOS
    • VIDEO
    • WIKI
  • BLOG
  • COMMUNITY
    • FACEBOOK
    • FORUM
    • INSTAGRAM
    • TWITTER
  • CONTACT US
  • HOME
  • NEWS
    • BIOENGINEERING
    • SCIENCE NEWS
  • EXPLORE
    • CAREER
      • Companies
      • Jobs
        • Lecturer
        • PhD Studentship
        • Postdoc
        • Research Assistant
    • EVENTS
    • iGEM
      • News
      • Team
    • PHOTOS
    • VIDEO
    • WIKI
  • BLOG
  • COMMUNITY
    • FACEBOOK
    • FORUM
    • INSTAGRAM
    • TWITTER
  • CONTACT US
No Result
View All Result
Bioengineer.org
No Result
View All Result
Home NEWS Science News Biology

Brain receptor pulls open electrical gate like a puppet master

Bioengineer by Bioengineer
June 30, 2020
in Biology
0
Share on FacebookShare on TwitterShare on LinkedinShare on RedditShare on Telegram

IMAGE

Credit: Furukawa lab/CSHL, 2020

For the first time, researchers in the lab of CSHL Professor Hiro Furukawa have been able to track each atom in the NMDA receptor, an important brain protein, as it transmits or inhibits neural signals. Critical for brain development and function, the receptor converts chemical messages between cells into electrical signals within a neuron. The key to transmitting that information is opening the receptor’s built-in ion channel, a hollow pore that allows electrically charged ions to flow. Unlocking the receptor’s ion channel is like working a stringed puppet–rock one part of the receptor and slender filaments pull open the channel’s gate. Rock it a little differently, the filaments loosen, and the gate snaps shut. Understanding how the receptor works could lead to better treatments for Alzheimer’s disease, depression, epilepsy, stroke, or schizophrenia.

Using high resolution electron cryo-microscopy (cryo-EM) and a series of specially constructed receptors, the scientists were able to follow every twist and turn of receptor parts as they bind natural and synthetic compounds, rock open the gate, and let it shut again.

The NMDA receptor is embedded in the neuronal membrane with the receptor binding portion on the outside of the cell and the ion channel spanning the cell membrane. When activating molecules glycine and glutamic acid bind to the ligand-binding domain (LBD) in the right way, the LBD rocks, pulling a loop or filament attached to the ion channel gate to open it. But if an antagonist binds, the loop loosens so much that the LBD cannot pull open the gate. Furukawa says:

“This is all happening because the subunit arrangement changes quite dramatically upon binding to the inhibitor. It all comes down to the stretching and non-stretching of the loop between the ligand-binding domain and the ion channel. They’re really a series of conformations or events that are happening outside [the cell], and it eventually gets translated to the ion channel activity,”

Formerly, the stretching of the loops and their effect on the opening and closing of the ion channel were pure speculation on Furukawa’s part. Now he has the data to prove what before he could only imagine.

Watch “How does the NMDA receptor work?”: https://www.youtube.com/watch?v=5zqBsPmH8ck

There are multiple conformations when glycine and glutamate are bound to NMDA receptor’s Ligand Binding Domain (LBD). In going from non-active to active state, there is going to be a rolling motion–I’m going to go back again–there’s going to be a rolling motion of Ligand Binding Domain. Here is the loop that tethers Ligand Binding Domain and a transmembrane domain. And the transmembrane domain forms the ion channel pore. When this rolling motion happens, it is that the loop that tethers that transmembrane domain would be stretched. When the loop is stretched, what happens is that the residues, or amino acids, that are forming the ion channel pore is stretched apart.

This discovery will enable researchers to develop better drugs to control the NMDA receptor’s activity, which can be involved in Alzheimer’s disease, depression, schizophrenia, stroke, and epilepsy. The insights gained in this study may also be applicable to other receptor-mediated ion channels.

###

Media Contact
Sara Roncero-Menendez
[email protected]

Original Source

https://www.cshl.edu/brain-receptor-pulls-open-electrical-gate-like-a-puppet-master/

Tags: AlzheimerBiologyMedicine/Healthneurobiology
Share12Tweet8Share2ShareShareShare2

Related Posts

IMAGE

No more needles for diagnostic tests?

January 22, 2021
IMAGE

Shift in caribou movements may be tied to human activity

January 22, 2021

Rediscovery of the ‘extinct’ Pinatubo volcano mouse

January 22, 2021

Meta-Apo supports cheaper, quicker microbiome functional assessment

January 22, 2021
Next Post
IMAGE

Plant tissue engineering improves drought and salinity tolerance

IMAGE

Study finds that plastic recycling from europe being dumped in Asian waters

Leave a Reply Cancel reply

Your email address will not be published.

This site uses Akismet to reduce spam. Learn how your comment data is processed.

POPULAR NEWS

  • IMAGE

    The map of nuclear deformation takes the form of a mountain landscape

    54 shares
    Share 22 Tweet 14
  • People living with HIV face premature heart disease and barriers to care

    65 shares
    Share 26 Tweet 16
  • New drug form may help treat osteoporosis, calcium-related disorders

    40 shares
    Share 16 Tweet 10
  • New findings help explain how COVID-19 overpowers the immune system

    35 shares
    Share 14 Tweet 9

About

We bring you the latest biotechnology news from best research centers and universities around the world. Check our website.

Follow us

Tags

Technology/Engineering/Computer ScienceBiologyClimate ChangePublic HealthMaterialsInfectious/Emerging DiseasesMedicine/HealthcancerGeneticsCell BiologyEcology/EnvironmentChemistry/Physics/Materials Sciences

Recent Posts

  • Regulating the ribosomal RNA production line
  • A professor from RUDN University developed new liquid crystals
  • New technique builds super-hard metals from nanoparticles
  • No more needles for diagnostic tests?
  • Contact Us

© 2019 Bioengineer.org - Biotechnology news by Science Magazine - Scienmag.

No Result
View All Result
  • Homepages
    • Home Page 1
    • Home Page 2
  • News
  • National
  • Business
  • Health
  • Lifestyle
  • Science

© 2019 Bioengineer.org - Biotechnology news by Science Magazine - Scienmag.

Welcome Back!

Login to your account below

Forgotten Password?

Create New Account!

Fill the forms below to register

All fields are required. Log In

Retrieve your password

Please enter your username or email address to reset your password.

Log In