Related Experiment Video

Updated: Oct 14, 2025

Dissection of Hippocampal Dentate Gyrus from Adult Mouse
07:42

Dissection of Hippocampal Dentate Gyrus from Adult Mouse

Published on: November 17, 2009

83.2K

Structure of the human Meckel-Gruber protein Meckelin

Dongliang Liu1,2,3, Dandan Qian4, Huaizong Shen1,2,3

  • 1Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang 310024, China.

Science Advances
|November 3, 2021
PubMed

Insights

Mutations in the Meckelin gene cause Meckel-Gruber syndrome. This study reveals the 3.3-Å cryo-EM structure of human Meckelin, providing insights into its function and disease mechanisms.

Area of Science:

  • Structural biology
  • Cell biology
  • Genetics

Background:

  • Meckel-Gruber syndrome is a severe ciliopathy with high mortality.
  • Mutations in the Meckelin gene are a primary cause of this syndrome.

Purpose of the Study:

  • To determine the high-resolution cryo-electron microscopy structure of human Meckelin (TMEM67/MKS3).
  • To provide a structural basis for understanding Meckelin function and its role in Meckel-Gruber syndrome.

Main Methods:

  • 3.3-Å cryo-electron microscopy (cryo-EM) was used to determine the structure of human Meckelin.
  • Analysis of the protein fold, including cysteine-rich, β sheet–rich, seven-transmembrane, and coiled-coil domains.

Main Results:

  • The structure reveals a unique protein fold with novel domains.
  • Meckelin possesses an unusual cysteine-rich domain, a β sheet–rich domain, a seven-transmembrane fold with a unique break, and a coiled-coil domain.
  • Meckelin forms a stable homodimer through an extensive interface.

Conclusions:

  • The determined structure provides a framework for understanding Meckelin's function.
  • This structural information is crucial for dissecting the molecular mechanisms underlying Meckel-Gruber syndrome.

More Related Videos

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

13.0K
Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium07:20

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium

Published on: April 9, 2019

9.3K

Related Concept Videos

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
4.3K
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
2.5K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
4.2K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
8.0K
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
28.9K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.8K