Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity

Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2011-03, Vol.108 (11), p.4322-4327
Main Authors: Baldock, Clair, Oberhauser, Andres F., Ma, Liang, Lammie, Donna, Siegler, Veronique, Mithieux, Suzanne M., Tu, Yidong, Chow, John Yuen Ho, Suleman, Farhana, Malfois, Marc, Rogers, Sarah, Guo, Liang, Irving, Thomas C., Wess, Tim J., Weiss, Anthony S., Tirrell, David A.
Format: Article
Language:English
Subjects:
Animals
Biological Sciences
Cells
Elastic tissue
Elasticity
Entropy
Exons
Human subjects
Humans
Hydrodynamics
Mechanical properties
Medical research
Models, Molecular
Molecular structure
Molecules
Monomers
Neutron Diffraction
Neutron scattering
Neutrons
Organ Specificity
Protein Conformation
Proteins
Scattering, Small Angle
Solutions
Studies
Tissues
Tropoelastin - chemistry
Vertebrates - metabolism
X-Ray Diffraction
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Elastin enables the reversible deformation of elastic tissues and can withstand decades of repetitive forces. Tropoelastin is the soluble precursor to elastin, the main elastic protein found in mammals. Little is known of the shape and mechanism of assembly of tropoelastin as its unique composition and propensity to self-associate has hampered structural studies. In this study, we solve the nanostructure of full-length and corresponding overlapping fragments of tropoelastin using small angle X-ray and neutron scattering, allowing us to identify discrete regions of the molecule. Tropoelastin is an asymmetric coil, with a protruding foot that encompasses the C-terminal cell interaction motif. We show that individual tropoelastin molecules are highly extensible yet elastic without hysteresis to perform as highly efficient molecular nanosprings. Our findings shed light on how biology uses this single protein to build durable elastic structures that allow for cell attachment to an appended foot. We present a unique model for head-to-tail assembly which allows for the propagation of the molecule's asymmetric coil through a stacked spring design.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1014280108