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STRUCTURAL BIOLOGY. Assembling the wheel of death.

08:00 EDT 23rd October 2015 | BioPortfolio

Summary of "STRUCTURAL BIOLOGY. Assembling the wheel of death."

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This article was published in the following journal.

Name: Science (New York, N.Y.)
ISSN: 1095-9203
Pages: 376-7

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Medical and Biotech [MESH] Definitions

A homotypic protein interaction module of the death domain superfamily that is composed of a bundle of six alpha-helices. The death effector domain shares sequence and structural similarities with the DEATH DOMAIN and CASPASE RECRUITMENT DOMAIN. It occurs in many proteins with essential functions in APOPTOSIS.

A conserved protein interaction domain of the death domain superfamily that is structurally similar to the DEATH EFFECTOR DOMAIN and CASPASE RECRUITMENT DOMAIN. Death domains bind each other to form oligomers and occur on DEATH DOMAIN RECEPTORS, where they are required for APOPTOSIS signaling and non-apoptotic functions.

The death of a FETUS of GESTATIONAL AGE 28 weeks or more, or the death of a live-born INFANT less than 28 days of age.

The field of biology which deals with the process of the growth and differentiation of an organism.

Complex compounds in which a dumbbell shaped molecule is encircled by a macrocycle. They are named after rota (wheel) and axis (axle). Notation with a prefix is used to indicate the number of interlocked components. They have potential use in NANOTECHNOLOGY. Rotaxanes have been made with CYCLODEXTRINS and CYCLIC ETHERS.

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