The SH3 domain of a M7 interacts with its C-terminal proline-rich region.

The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Research Abstract Details 

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The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Abstract Text:

Qinghua Wang,Matthew A Deloia,Yang Kang,Casey Litchke,Naixia Zhang,Margaret A Titus,Kylie J Walters,

Myosins play essential roles in migration, cytokinesis, endocytosis, and adhesion. They are composed of a large N-terminal motor domain with ATPase and actin binding sites and C-terminal neck and tail regions, whose functional roles and structural context in the protein are less well characterized. The tail regions of myosins I, IV, VII, XII, and XV each contain a putative SH3 domain that may be involved in protein-protein interactions. SH3 domains are reported to bind proline-rich motifs, especially "PxxP" sequences, and such interactions serve regulatory functions. The activity of Src, PI3, and Itk kinases, for example, is regulated by intramolecular interactions between their SH3 domain and internal proline-rich sequences. Here, we use NMR spectroscopy to reveal the structure of a protein construct from Dictyostelium myosin VII (DdM7) spanning A1620-T1706, which contains its SH3 domain and adjacent proline-rich region. The SH3 domain forms the signature beta-barrel architecture found in other SH3 domains, with conserved tryptophan and tyrosine residues forming a hydrophobic pocket known to bind "PxxP" motifs. In addition, acidic residues in the RT or n-Src loops are available to interact with the basic anchoring residues that are typically found in ligands or proteins that bind SH3 domains. The DdM7 SH3 differs in the hydrophobicity of the second pocket formed by the 3(10) helix and following beta-strand, which contains polar rather than hydrophobic side chains. Most unusual, however, is that this domain binds its adjacent proline-rich region at a surface remote from the region previously identified to bind "PxxP" motifs. The interaction may affect the orientation of the tail without sacrificing the availability of the canonical "PxxP"-binding surface.

The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Publishing Authors By Initials

Q Wang,MA Deloia,Y Kang,C Litchke,N Zhang,MA Titus,KJ Walters,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research

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The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Protein science : a publication of the Protein Soc

VOLUME: 16

Page Numbers: 189-96

Journal Abbreviation: Protein Sci.

ISSN: 0961-8368

DAY: 22

MONTH: 12

YEAR: 2006

The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9211750

The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Keywords Mesh Terms:

KEYWORDS: src Homology Domains

MESH TERMS: metabolism

Chemical & Substance for Abstract: The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for The SH3 domain of a M7 interacts with its C-terminal proline-rich region.

AFFILIATION: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM 046486

ACRONYM: GM

MEDLINETA: Protein Sci

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