Structural and mechanistic principles of intramembrane proteolysis lessons from rhomboids

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00392839" target="_blank" >RIV/61388963:_____/13:00392839 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1111/febs.12199" target="_blank" >http://dx.doi.org/10.1111/febs.12199</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.12199" target="_blank" >10.1111/febs.12199</a>

Result language

angličtina

Original language name

Structural and mechanistic principles of intramembrane proteolysis lessons from rhomboids

Original language description

Intramembrane proteases cleave membrane proteins in their transmembrane helices to regulate a wide range of biological processes. They catalyse hydrolytic reactions within the hydrophobic environment of lipid membranes where water is normally excluded. How? Do the different classes of intramembrane proteases share any mechanistic principles? In this review these questions will be discussed in view of the crystal structures of prokaryotic members of the three known catalytic types of intramembrane proteases published over the past 7years. Rhomboids, the intramembrane serine proteases that are the best understood family, will be the initial area of focus, and the principles that have arisen from a number of structural and biochemical studies will be considered. The site-2 metalloprotease and GXGD-type aspartyl protease structures will then be discussed, with parallels drawn and differences highlighted between these enzymes and the rhomboids. Despite the significant advances achieved so f

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2013

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

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Volume of the periodical

280

Issue of the periodical within the volume

7

Country of publishing house

GB - UNITED KINGDOM

Number of pages

25

Pages from-to

1579-1603

UT code for WoS article

000316913500001

EID of the result in the Scopus database

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