Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F08%3A00005478" target="_blank" >RIV/61989592:15310/08:00005478 - isvavai.cz</a>

Result on the web

—

DOI - Digital Object Identifier

—

Result language

angličtina

Original language name

Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation

Original language description

Cyclin-dependent kinase 2 (CDK2) is the most thoroughly studied of the cyclin-dependent kinases that regulate essential cellular processes, including the cell cycle, and it has become a model for studies of regulatory mechanisms at the molecular level. This contribution identifies flexible and rigid regions of CDK2 based on temperature B-factors acquired from both X-ray data and molecular dynamics simulations. In addition, the biological relevance of the identified flexible regions and their motions isexplored using information from the essential dynamics analysis related to conformational changes of CDK2 and knowledge of its biological function(s). The conserved regions of CMGC protein kinases' primary sequences are located in the most rigid regionsidentified in our analyses, with the sole exception of the absolutely conserved G13 in the tip of the glycine-rich loop. The conserved rigid regions are important for nucleotide binding, catalysis, and substrate recognition. In contrast,

Czech name

Funkční flexibilita lidské cyklin-dependentní kinasy-2 její evoluční konzervace

Czech description

Práce identifikuje flexibilní regiony lidské CDK2, uvádí jejich biologickou roli a evoluční konzervaci mezi CMGC kinasami.

Type

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

CEP classification

CF - Physical chemistry and theoretical chemistry

OECD FORD branch

—

Project

<a href="/en/project/LC512" target="_blank" >LC512: Center for biomolecules and complex molecular systems</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2008

Confidentiality

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

Name of the periodical

Protein Science

ISSN

0961-8368

e-ISSN

—

Volume of the periodical

17

Issue of the periodical within the volume

1

Country of publishing house

US - UNITED STATES

Number of pages

12

Pages from-to

—

UT code for WoS article

—

EID of the result in the Scopus database

—