Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turn-containing crosslinking domain

L B Dyksterhuis; Clair Baldock; Donna Lammie; Tim J Wess; A S Weiss

doi:10.1016/j.matbio.2006.10.002

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Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turn-containing crosslinking domain

Journal article

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Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turn-containing crosslinking domain

L B Dyksterhuis, Clair Baldock, Donna Lammie, Tim J Wess and A S Weiss

Matrix Biology, Vol.26(2), pp.125-135

2007

DOI: https://doi.org/10.1016/j.matbio.2006.10.002

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Abstract

tropoelastin

coacervation

polymerization

circular dichroism

mass spectrometry

small angle X-ray scattering

structure

The central region of tropoelastin including domains 19-25 of human tropoelastin forms a hot-spot for contacts during the inter-molecular association of tropoelastin by coacervation [Wise, S.G., Mithieux, S.M., Raftery, M.J. and Weiss, A.S (2005). "Specificity in the coacervation of tropoelastin: solvent exposed lysines." Journal of Structural Biology 149: 273-81.]. We explored the physical properties of this central region using a sub-fragment bordered by domains 17-27 of human tropoelastin (SHEL 17-27) and identified the intra- and inter-molecular contacts it forms during coacervation. A homobifunctional amine reactive crosslinker (with a maximum reach of 11 Ã…, corresponding to ∼ 7 residues in an extended polypeptide chain) was used to capture these contacts and crosslinked regions were identified after protease cleavage and mass spectrometry (MS) with MS/MS verification. An intermolecular crosslink formed between the lysines at positions 353 of each strand of tropoelastin at the lowest of crosslinker concentrations and was observed in all samples tested, suggesting that this residue forms an important initial contact during coacervation. At higher crosslinker concentrations, residues K425 and K437 showed the highest levels of involvement in crosslinks. An intramolecular crosslink between these K425 and K437, separated by 11 residues, indicated that a structural bend must serve to bring these residues into close proximity. These studies were complemented by small angle X-ray scattering studies that confirmed a bend in this important subfragment of the tropoelastin molecule. © 2006 International Society of Matrix Biology.

Details

Title: Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turn-containing crosslinking domain
Authors: L B Dyksterhuis (Author) - University of Sydney
Clair Baldock (Author) - University of Manchester, United Kingdom
Donna Lammie (Author) - Cardiff University, United Kingdom
Tim J Wess (Author) - Cardiff University, United Kingdom
A S Weiss (Author) - University of Sydney
Publication details: Matrix Biology, Vol.26(2), pp.125-135
Publisher: Elsevier BV
Date published: 2007
DOI: 10.1016/j.matbio.2006.10.002
ISSN: 0945-053X
Organisation Unit: Office of the Deputy Vice-Chancellor (Academic); University of the Sunshine Coast, Queensland
Language: English
Record Identifier: 99451254602621
Output Type: Journal article

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