English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure and dynamics of the human muscle LIM protein

Schallus, T., Fehér, K., Ulrich, A. S., Stier, G., & Muhle-Goll, C. (2009). Structure and dynamics of the human muscle LIM protein. FEBS Letters, 583(6), 1017-1022. doi:10.1016/j.febslet.2009.02.021.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-15DB-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-DED4-7
Genre: Journal Article

Files

show Files
hide Files
:
FEBSLett_583_2009_1017.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
FEBSLett_583_2009_1017.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Schallus, Thomas1, Author              
Fehér, Krisztina1, Author              
Ulrich, Anne S., Author
Stier, Gunter1, Author              
Muhle-Goll, Claudia1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: Cysteine rich protein; NMR; α-Actinin; Telethonin
 Abstract: The family of cysteine rich proteins (CRP) comprises three closely homologous members that have been reported to interact with alpha-actinin. Muscular LIM protein (MLP/CRP3), the skeletal muscle variant, was originally discovered as a positive regulator of myogenesis and is suggested to be part of the stretch sensor of the myofibril through its interaction with telethonin (T-Cap). We determined the structure of both LIM domains of human MLP by nuclear magnetic resonance spectroscopy. We confirm by (15)N relaxation measurements that both LIM domains act as independent units and that the adjacent linker regions are fully flexible. With the published structures of CRP1 and CRP2, the complete family has now been structurally characterized.

Details

show
hide
Language(s): eng - English
 Dates: 2009-02-102008-12-222009-02-112009-02-212009-03-18
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 583 (6) Sequence Number: - Start / End Page: 1017 - 1022 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501