Comparative genomics of elastin: Sequence analysis of a highly repetitive protein

He, David; Chung, Martin; Chan, Esther T.; Alleyne, Trevis M.; Ha, Kevin C.H.; Miao, Ming; Stahl, Richard; Keeley, Fred W.; Parkinson, John

doi:10.1016/j.matbio.2007.05.005

Cited by 66 publications

(73 citation statements)

References 52 publications

(74 reference statements)

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“…KA-type cross-linking domains are abundant and well conserved in tropoelastins of most species (32)(33)(34). Although lysine-derived cross-links generated by the action of lysyl oxidase are also present in collagens, elastomeric proteins of nonvertebrates use other cross-linking mechanisms to stabilize their polymeric structures.…”

Section: Lysine Point Mutations Induce ␤-Sheet Secondary Structure Inmentioning

confidence: 99%

“…As a result, the current model for elastin assembly considers the cross-linking domains as relatively passive participants in the process, maintaining ␣-helical structure throughout assembly from monomer to coacervate to cross-linked polymer. However, formation of lysine-derived cross-links by these KA-type cross-linking domains is strongly conserved in elastins across vertebrate phylogeny (32)(33)(34), suggesting these sequences provide particular advantages to assembly. Furthermore, although they do not coacervate on their own, we and others have shown that the sequence and arrangements of the cross-linking domains within elastin-like polypeptides can have a dramatic effect on their coacervation characteristics (17).…”

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confidence: 99%

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Conformational Transitions of the Cross-linking Domains of Elastin during Self-assembly

Reichheld

Muiznieks

Stahl

et al. 2014

Journal of Biological Chemistry

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Background: Elastin is a polymeric protein providing extensibility and elastic recoil to tissues. Results: Cross-linking domain structure shifts from random coil to ␤-strand to ␣-helix during assembly of elastin matrix. Conclusion: Cross-linking domains have a previously unappreciated structural lability during assembly, which is highly susceptible to mutations of lysine residues. Significance: Identification of conformational transitions in cross-linking domains of elastin during self-assembly is essential for understanding the mechanisms of formation of the elastic matrix.

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Section: Lysine Point Mutations Induce ␤-Sheet Secondary Structure Inmentioning

confidence: 99%

mentioning

confidence: 99%

Conformational Transitions of the Cross-linking Domains of Elastin during Self-assembly

Reichheld

Muiznieks

Stahl

et al. 2014

Journal of Biological Chemistry

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“…For example, resilin is found in insect cuticles and wings where it allows stretching in response to beats (2)(3)(4). Elastin in the human blood vessels is able to react to changes in blood pressure and confers elasticity to skin, tendons, and lungs (5)(6)(7). Keratin is the building fiber of external animal structures such as hairs, nails, claws, horns, wool, feathers and hoofs, whereas collagen is an abundant structural protein important to several tissues, including bone, teeth, tendons, and cartilage.…”

Section: Introductionmentioning

confidence: 99%

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Arnold

Marcotte

2009

Concepts Magnetic Resonance

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As a consequence of evolutionary pressure, various organisms have developed structural fibers displaying a range of exceptional mechanical properties adapted specifically to their functions. An understanding of these properties at the molecular level requires a detailed description of local structure, orientation with respect to the fiber and size of constitutive units, and dynamics on various timescales. The size and lack of long-range order in these protein systems constitute an important challenge to classical structural techniques such as high-resolution NMR and X-ray diffraction. Solidstate NMR overcomes these constraints and is uniquely suited to the study of these inherently disordered systems. Solid-state NMR experiments developed or applied to determine structure, orientation, and dynamics of these complex proteins will be reviewed and illustrated through examples of their applications to fibers such as spider and silkworm silks, collagen, elastin, and keratin.

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“…Tropoelastin is the fundamental building component of all elastins. The most important feature of the primary tropoelastin sequence is the distinct arrangement of alternating hydrophobic and cross-linking domains which is highly conserved in elastins from all species (Chung et al, 2006;He et al, 2007). Further, tropoelastin has the ability to selfassemble under physiological conditions and exhibit an inverse temperature transition (ITT) behavior.…”

Section: Introductionmentioning

confidence: 99%

Elastin-like polypeptides and their applications in anticancer drug delivery systems: a review

Saxena

Nanjan

2013

Drug Delivery

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Elastin-like polypeptides (ELPs) are large molecular weight biopolymers. They have been widely studied as macromolecular carriers for targeted delivery of drugs. The aim of the present article is to review the available information on ELPs (including our recent investigations), their properties, drug delivery applications to tumor sites and future perspectives. This review also provides information on the use of short synthetic ELPs for making ELP-drug conjugates, for targeted delivery of anticancer drugs. In the present review we also focus on the point that short ELPs can also be used for targeting anticancer drugs to tumor sites as they behave similar to long ELPs regarding their capacity to undergo inverse temperature transition (ITT) behavior.

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Comparative genomics of elastin: Sequence analysis of a highly repetitive protein

Cited by 66 publications

References 52 publications

Conformational Transitions of the Cross-linking Domains of Elastin during Self-assembly

Conformational Transitions of the Cross-linking Domains of Elastin during Self-assembly

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Elastin-like polypeptides and their applications in anticancer drug delivery systems: a review

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