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Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy

BACKGROUND: Protein tyrosine kinases are involved in signal transduction pathways that regulate cell growth, differentiation, activation and transformation. Human lymphocyte specific kinase (Lck) is a 56 kDa protein involved in T-cell- and IL2-receptor signaling. Three-dimensional structures are kno...

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Detalles Bibliográficos
Autores principales: Briese, Lars, Willbold, Dieter
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC156628/
https://www.ncbi.nlm.nih.gov/pubmed/12734017
http://dx.doi.org/10.1186/1472-6807-3-3
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author Briese, Lars
Willbold, Dieter
author_facet Briese, Lars
Willbold, Dieter
author_sort Briese, Lars
collection PubMed
description BACKGROUND: Protein tyrosine kinases are involved in signal transduction pathways that regulate cell growth, differentiation, activation and transformation. Human lymphocyte specific kinase (Lck) is a 56 kDa protein involved in T-cell- and IL2-receptor signaling. Three-dimensional structures are known for SH3, SH2 and kinase domains of Lck as well as for other tyrosine kinases. No structure is known for the unique domain of any Src-type tyrosine kinase. RESULTS: Lck(1–120) comprising unique and SH3 domains was structurally investigated by nuclear magnetic resonance spectroscopy. We found the unique domain, in contrast to the SH3 part, to have basically no defined structural elements. The solution structure of the SH3 part could be determined with very high precision. It does not show significant differences to Lck SH3 in the absence of the unique domain. Minor differences were observed to the X-ray structure of Lck SH3. CONCLUSION: The unique domain of Lck does not contain any defined structure elements in the absence of ligands and membranes. Presence of the unique domain is not relevant to the three-dimensional structure of the Lck SH3 domain.
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spelling pubmed-1566282003-06-05 Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy Briese, Lars Willbold, Dieter BMC Struct Biol Research Article BACKGROUND: Protein tyrosine kinases are involved in signal transduction pathways that regulate cell growth, differentiation, activation and transformation. Human lymphocyte specific kinase (Lck) is a 56 kDa protein involved in T-cell- and IL2-receptor signaling. Three-dimensional structures are known for SH3, SH2 and kinase domains of Lck as well as for other tyrosine kinases. No structure is known for the unique domain of any Src-type tyrosine kinase. RESULTS: Lck(1–120) comprising unique and SH3 domains was structurally investigated by nuclear magnetic resonance spectroscopy. We found the unique domain, in contrast to the SH3 part, to have basically no defined structural elements. The solution structure of the SH3 part could be determined with very high precision. It does not show significant differences to Lck SH3 in the absence of the unique domain. Minor differences were observed to the X-ray structure of Lck SH3. CONCLUSION: The unique domain of Lck does not contain any defined structure elements in the absence of ligands and membranes. Presence of the unique domain is not relevant to the three-dimensional structure of the Lck SH3 domain. BioMed Central 2003-05-07 /pmc/articles/PMC156628/ /pubmed/12734017 http://dx.doi.org/10.1186/1472-6807-3-3 Text en Copyright © 2003 Briese and Willbold; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research Article
Briese, Lars
Willbold, Dieter
Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
title Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
title_full Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
title_fullStr Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
title_full_unstemmed Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
title_short Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
title_sort structure determination of human lck unique and sh3 domains by nuclear magnetic resonance spectroscopy
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC156628/
https://www.ncbi.nlm.nih.gov/pubmed/12734017
http://dx.doi.org/10.1186/1472-6807-3-3
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