Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip.

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Abstract Text:

David D Weis,Peter Kjellen,Bartholomew M Sefton,John R Engen,

The Tip protein from Herpesvirus saimiri interacts with the SH3 domain from the Src-family kinase Lck via a proline-containing sequence termed LBD1. Src-family kinase SH3 domains related to Lck have been shown to be dynamic in solution and partially unfold under physiological conditions. The rate of such partial unfolding is reduced by viral protein binding. To determine if the Lck SH3 domain displayed similar behavior, the domain was investigated with hydrogen exchange and mass spectrometry. Lck SH3 was found to be highly dynamic in solution. While other SH3 domains require as much as 10,000 sec to become totally deuterated, Lck SH3 became almost completely labeled within 200 sec. A partial unfolding event involving 8-10 residues was observed with a half-life of approximately 10 sec. Tip LBD1 binding did not cause gross structural changes in Lck SH3 but globally stabilized the domain and reduced the rate of partial unfolding by a factor of five. The region of partial unfolding in Lck SH3 was found to be similar to that identified for other SH3 domains that partially unfold. Although the sequence conservation between Lck SH3 and other closely related SH3 domains is high, the dynamics do not appear to be conserved.

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Publishing Authors By Initials

DD Weis,P Kjellen,BM Sefton,JR Engen,

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

PUBMED ID PMID:

MEDLINE DATE:

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Protein science : a publication of the Protein Soc

VOLUME: 15

Page Numbers: 2402-10

Journal Abbreviation: Protein Sci.

ISSN: 0961-8368

DAY: 3

MONTH: Oct

YEAR: 2006

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9211750

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Keywords Mesh Terms:

KEYWORDS: src Homology Domains

MESH TERMS: metabolism

Chemical & Substance for Abstract: Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Information

Substance Name: Lymphocyte Specific Protein Tyrosine Kin

Registry Number: EC 2.7.1.37

Grant and Affiliation Information for Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip.

AFFILIATION: Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01-GM070590

ACRONYM: GM

MEDLINETA: Protein Sci

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip Related Publications

• Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip.
• Associations to odors: interference, mnemonics, and verbal labeling.
• Asymmetric competition drives lake use of coexisting salmonids.
• DEVELOPMENT OF EXTERNALLY POWERED UPPER EXTREMITY ORTHOTIC SYSTEMS.
• Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.
• Heterogeneity in dynamic species abundance models: The selective effect of extinction processes.
• Heterogeneous communities with lognormal species abundance distribution: Species-area curves and sustainability.
• High-speed and high-resolution UPLC separation at zero degrees celsius.
• Ion mobility adds an additional dimension to mass spectrometric analysis of solution-phase hydrogen/deuterium exchange.
• Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii.
• Statistical derivation of a standardised procedure for counting expectorated alveolar macrophages as indicators of occupational air pollution.
• The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.
• [Epidemiological aspects of AIDS--some statistical examples]
• [Private hospitals and cosmetic surgery]