NMR characterization of the near native and unfolded states of the PTB domain of Dok1 : alternate conformations and residual clusters
Background: Phosphotyrosine binding (PTB) domains are critically involved in cellular signaling and diseases. PTB domains are categorized into three distinct structural classes namely IRS-like, Shc-like and Dab-like. All PTB domains consist of a core pleckstrin homology (PH) domain with additional...
Main Authors: | Gupta, Sebanti, Bhattacharjya, Surajit |
---|---|
Other Authors: | Driscoll, Paul C. |
Format: | Journal Article |
Language: | English |
Published: |
2014
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/102910 http://hdl.handle.net/10220/19074 |
Similar Items
-
Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
by: Sebanti Gupta
Published: (2014) -
An alternative phosphorylation switch in integrin β2 (CD18) tail for Dok1 binding
by: Gupta, Sebanti, et al.
Published: (2015) -
Salt dependence conformational stability of the dimeric SAM domain of MAPKKK Ste11 from budding yeast : a native-state H/D exchange NMR Study
by: Bhunia, Anirban, et al.
Published: (2021) -
β-hairpin peptides : heme binding, catalysis, and structure in detergent micelles
by: Mahajan, Mukesh, et al.
Published: (2013) -
Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS
by: Gozani, Shai N., et al.
Published: (2012)