Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility.
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Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1ELigand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1Beyond the binding site: the role of the β₂-β₃ loop and extra-domain structures in PDZ domainsChange in allosteric network affects binding affinities of PDZ domains: analysis through perturbation response scanning.Protein binding specificity versus promiscuity.Investigating Dynamic Interdomain Allostery in Pin1Sequence-specific long range networks in PSD-95/discs large/ZO-1 (PDZ) domains tune their binding selectivity.Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions.Hidden electrostatic basis of dynamic allostery in a PDZ domain.
P2860
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P2860
Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Conserved tertiary couplings s ...... in conformational flexibility.
@ast
Conserved tertiary couplings s ...... in conformational flexibility.
@en
type
label
Conserved tertiary couplings s ...... in conformational flexibility.
@ast
Conserved tertiary couplings s ...... in conformational flexibility.
@en
prefLabel
Conserved tertiary couplings s ...... in conformational flexibility.
@ast
Conserved tertiary couplings s ...... in conformational flexibility.
@en
P2860
P356
P1433
P1476
Conserved tertiary couplings s ...... in conformational flexibility.
@en
P2093
Bosco K Ho
David A Agard
P2860
P304
P356
10.1002/PRO.318
P577
2010-03-01T00:00:00Z