Related Experiment Video

Updated: Jun 17, 2026

Biological Preparation and Mechanical Technique for Determining Viscoelastic Properties of Zonular Fibers
06:39

Biological Preparation and Mechanical Technique for Determining Viscoelastic Properties of Zonular Fibers

Published on: December 16, 2021

[Computer construction and analysis of protein models of mutant fibrillin-1 gene in Marfan's syndrome]

Xing-chao Shentu1, Xia-jing Tang, Pan-pan Ye

  • 1Eye Center, Second Affiliated Hospital, Zhejiang University College of Medicine, Hangzhou 310009, China.

[Zhonghua Yan Ke Za Zhi] Chinese Journal of Ophthalmology
|December 22, 2009
PubMed
Abstract

Insights

Computer analysis of fibrillin-1 (FBN1) gene mutations reveals significant structural changes in FBN1 protein. These alterations in FBN1 protein structure are linked to the development of ectopia lentis in patients.

Area of Science:

  • Molecular biology
  • Genetics
  • Structural biology

Background:

  • Fibrillin-1 (FBN1) is crucial for extracellular microfibrils and implicated in Marfan syndrome (MFS).
  • Specific FBN1 mutations, Arg545Cys and Arg1530Cys, are associated with ectopia lentis in Chinese patients.

Purpose of the Study:

  • To analyze the structural impact of Arg545Cys and Arg1530Cys mutations in the FBN1 gene.
  • To understand the molecular pathogenesis of ectopia lentis linked to FBN1 mutations.

Main Methods:

  • Protein models of mutant FBN1 genes (Arg545Cys and Arg1530Cys) were constructed.
  • Protein structures were predicted using SWISS-MODEL and visualized with Swiss-Pdb Viewer.

Main Results:

  • The Arg545Cys FBN1 mutation altered secondary structure, reduced hydrogen bond distance, changed solvent accessibility, and decreased negative electrostatic potential.
  • The Arg1530Cys FBN1 mutation resulted in lost hydrogen bonds, altered solvent accessibility, and increased negative electrostatic potential.

Conclusions:

  • Computational analysis demonstrates significant secondary structure alterations in FBN1 protein due to these mutations.
  • This study supports the role of mutant FBN1 in the pathogenesis of human ectopia lentis.

More Related Videos

Aip1p Dynamics Are Altered by the R256H Mutation in Actin08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Preparation of 3D Decellularized Matrices from Fetal Mouse Skeletal Muscle for Cell Culture07:44

Preparation of 3D Decellularized Matrices from Fetal Mouse Skeletal Muscle for Cell Culture

Published on: March 3, 2023

Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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 form...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...