The catalytic domain of MMP-1 studied through tagged lanthanides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10119150" target="_blank" >RIV/00216208:11310/12:10119150 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.febslet.2011.09.020" target="_blank" >http://dx.doi.org/10.1016/j.febslet.2011.09.020</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.febslet.2011.09.020" target="_blank" >10.1016/j.febslet.2011.09.020</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The catalytic domain of MMP-1 studied through tagged lanthanides

Popis výsledku v původním jazyce

Pseudocontact shifts (pcs) and paramagnetic residual dipolar couplings (rdc) provide structural information that can be used to assess the adequacy of a crystallographic structure to represent the solution structure of a protein. This can be done by attaching a lanthanide binding tag to the protein. There are cases in which only local rearrangements are sufficient to match the NMR data and cases where significant secondary structure or domain rearrangements from the solid state to the solution state areneeded. We show that the two cases are easily distinguishable. Whereas the use of solution restraints in the latter case is described in the literature, here we deal with how to obtain a better model of the solution structure in a case (the catalytic domain of the matrix metalloproteinase MMP-1) of the former class.

Název v anglickém jazyce

The catalytic domain of MMP-1 studied through tagged lanthanides

Popis výsledku anglicky

Pseudocontact shifts (pcs) and paramagnetic residual dipolar couplings (rdc) provide structural information that can be used to assess the adequacy of a crystallographic structure to represent the solution structure of a protein. This can be done by attaching a lanthanide binding tag to the protein. There are cases in which only local rearrangements are sufficient to match the NMR data and cases where significant secondary structure or domain rearrangements from the solid state to the solution state areneeded. We show that the two cases are easily distinguishable. Whereas the use of solution restraints in the latter case is described in the literature, here we deal with how to obtain a better model of the solution structure in a case (the catalytic domain of the matrix metalloproteinase MMP-1) of the former class.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CA - Anorganická chemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

FEBS Letters

ISSN

0014-5793

e-ISSN

—

Svazek periodika

586

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

557-567

Kód UT WoS článku

000301222900014

EID výsledku v databázi Scopus

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