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Related Concept Videos

Internal Receptors01:31

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
Short-distance Transport of Resources02:12

Short-distance Transport of Resources

Short-distance transport refers to transport that occurs over a distance of just 2-3 cells, crossing the plasma membrane in the process. Small uncharged molecules, such as oxygen, carbon dioxide, and water, can diffuse across the plasma membrane on their own. In contrast, ions and larger molecules require the assistance of transport proteins due to their charge or size. Transport across membranes also occurs within individual cells, playing a variety of essential roles for the plant as a whole.
Riboswitches01:56

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Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
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Channel Rhodopsins01:11

Channel Rhodopsins

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Cell Signaling in Plants01:25

Cell Signaling in Plants

Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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Structural insight into brassinosteroid perception by BRI1.

Ji She1, Zhifu Han, Tae-Wuk Kim

  • 1Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University, Beijing 100084, China.

Nature
|June 14, 2011
PubMed
Summary
This summary is machine-generated.

Plant hormones called brassinosteroids are key for growth. Researchers discovered how the BRI1 receptor recognizes brassinolide through structural analysis, revealing the molecular basis for plant hormone signaling.

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Area of Science:

  • Plant Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Brassinosteroids are essential plant hormones regulating growth and development.
  • Hormone perception involves the BRASSINOSTEROID-INSENSITIVE 1 (BRI1) receptor complex.
  • BRI1 recognizes brassinosteroids via its extracellular leucine-rich repeat (LRR) domain, initiating signaling cascades.

Purpose of the Study:

  • To elucidate the molecular mechanism of brassinosteroid recognition by BRI1.
  • To determine the crystal structures of the BRI1 LRR domain in its free and ligand-bound states.
  • To provide structural insights into brassinosteroid-induced receptor activation.

Main Methods:

  • X-ray crystallography was used to determine the structures of BRI1(LRR).
  • Structural analysis of BRI1(LRR) in both apo and brassinolide-bound forms.
  • Biochemical assays to confirm monomeric state and ligand binding.

Main Results:

  • BRI1(LRR) functions as a monomer, independent of brassinolide binding.
  • The structure reveals a helical solenoid with an insertion domain, forming a binding groove.
  • Brassinolide binds within this groove via an induced-fit mechanism, stabilizing interdomain loops.

Conclusions:

  • The study defines the structural basis for brassinosteroid recognition by the BRI1 receptor.
  • An induced-fit mechanism involving loop stabilization facilitates hormone binding.
  • These findings offer crucial insights into the initial steps of brassinosteroid signaling and receptor activation.