Crystal structure of the PB1 domain of NBR1

The scaffold protein NBR1 is involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Its N-terminal Phox and Bem1p (PB1) domain plays a critical role in mediating protein–protein interactions with both titin kinase and with another scaffold protei...

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Bibliographic Details
Published inFEBS letters Vol. 580; no. 1; pp. 341 - 344
Main Authors Müller, Simone, Kursula, Inari, Zou, Peijian, Wilmanns, Matthias
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 09.01.2006
Subjects
Connectin
Crystallography, X-Ray
Humans
Muscle Proteins - metabolism
PB1 domain
Protein Binding - physiology
Protein Kinases - metabolism
Protein Structure, Tertiary
Proteins - chemistry
Proteins - metabolism
Signal transduction
Signal Transduction - physiology
Titin
X-ray crystallography
X-ray crystallography
Signal transduction
PB1 domain
Titin
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Summary:The scaffold protein NBR1 is involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Its N-terminal Phox and Bem1p (PB1) domain plays a critical role in mediating protein–protein interactions with both titin kinase and with another scaffold protein, p62. We have determined the crystal structure of the PB1 domain of NBR1 at 1.55 Å resolution. It reveals a type-A PB1 domain with two negatively charged residue clusters. We provide a structural perspective on the involvement of NBR1 in the titin kinase signalling pathway.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2005.12.021