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

被引：149

作者：

Baldock, Clair ^{[2
]}

Oberhauser, Andres F. ^{[3
]}

Ma, Liang ^{[3
]}

Lammie, Donna ^{[4
]}

Siegler, Veronique ^{[4
]}

Mithieux, Suzanne M. ^{[1
]}

Tu, Yidong ^{[1
]}

Chow, John Yuen Ho ^{[1
]}

Suleman, Farhana ^{[2
]}

Malfois, Marc ^{[5
]}

Rogers, Sarah ^{[6
]}

Guo, Liang ^{[7
,8
]}

Irving, Thomas C. ^{[7
,8
]}

Wess, Tim J. ^{[4
]}

Weiss, Anthony S. ^{[1
]}

机构：

[1] Univ Sydney, Sch Mol Biosci, Sydney, NSW 2006, Australia

[2] Univ Manchester, Wellcome Trust Ctr Cell Matrix Res, Fac Life Sci, Manchester M13 9PT, Lancs, England

[3] Univ Texas Med Branch, Dept Neurosci & Cell Biol, Sealy Ctr Struct Biol & Mol Biophys, Galveston, TX 77555 USA

[4] Cardiff Univ, Sch Optometry & Vis Sci, Cardiff CF24 4LU, S Glam, Wales

[5] Diamond Light Source Ltd, Didcot OX11 0DE, Oxon, England

[6] ISIS Sci & Technol Facil Council, Didcot OX11 0QX, Oxon, England

[7] IIT, BioCAT, Ctr Synchrotron Radiat Res & Instrumentat, Chicago, IL 60616 USA

[8] IIT, Dept Biol Chem & Phys Sci, Chicago, IL 60616 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2011年 / 108卷 / 11期

基金：

英国医学研究理事会; 美国国家卫生研究院; 澳大利亚研究理事会;

关键词：

AFM; SAXS; atomic force microscopy; SMALL-ANGLE SCATTERING; RAY SOLUTION SCATTERING; CROSS-LINKING DOMAIN; MECHANICAL-PROPERTIES; MOLECULAR ELASTICITY; ESCHERICHIA-COLI; COACERVATION; SYSTEM; MICROFIBRILS; POLYPEPTIDES;

D O I：

10.1073/pnas.1014280108

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

070301 [无机化学]; 070403 [天体物理学]; 070507 [自然资源与国土空间规划学]; 090105 [作物生产系统与生态工程];

摘要：

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.

引用

页码：4322 / 4327

页数：6

共 60 条

[1]

Cell Adhesion to Tropoelastin Is Mediated via the C-terminal GRKRK Motif and Integrin αVβ3 [J].