NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding.
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Force and Compliance Measurements on Living Cells Using Atomic Force Microscopy (AFM).Molecular characterisation of the caprine (Capra hircus) lymphocyte function-associated antigen-1 alpha subunit-encoding cDNA.An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domainStructures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation.Structure of an integrin with an αI domain, complement receptor type 4An internal ligand-bound, metastable state of a leukocyte integrin, α X β 2Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive stateRGD-containing peptides inhibit fibrinogen binding to platelet alpha(IIb)beta3 by inducing an allosteric change in the amino-terminal portion of alpha(IIb)Structural basis of integrin regulation and signalingSmall-molecule inhibitors of protein-protein interactions: progressing towards the dreamA small molecule agonist of an integrin, alphaLbeta2.Dynamic shifts in LFA-1 affinity regulate neutrophil rolling, arrest, and transmigration on inflamed endothelium.Distinct roles for LFA-1 affinity regulation during T-cell adhesion, diapedesis, and interstitial migration in lymph nodes.Small molecule agonists of integrin CD11b/CD18 do not induce global conformational changes and are significantly better than activating antibodies in reducing vascular injury.Identification and characterization of a human monoclonal antagonistic antibody AL-57 that preferentially binds the high-affinity form of lymphocyte function-associated antigen-1.High-throughput screening based identification of small molecule antagonists of integrin CD11b/CD18 ligand binding.Molecular mechanism of alpha2beta1 integrin interaction with human echovirus 1.Integrin α2β1 in nonactivated conformation can induce focal adhesion kinase signalingAn isolated, surface-expressed I domain of the integrin alphaLbeta2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond.Directed evolution to probe protein allostery and integrin I domains of 200,000-fold higher affinity.Two-dimensional kinetics regulation of alphaLbeta2-ICAM-1 interaction by conformational changes of the alphaL-inserted domainIntegrin structure: new twists and turns in dynamic cell adhesion.Utilization of I-domain of LFA-1 to Target Drug and Marker Molecules to Leukocytes.Regulation of outside-in signaling and affinity by the beta2 I domain of integrin alphaLbeta2.AL-57, a ligand-mimetic antibody to integrin LFA-1, reveals chemokine-induced affinity up-regulation in lymphocytes.Integrins, cations and ligands: making the connection.Importance of force linkage in mechanochemistry of adhesion receptors.The C-terminal αI domain linker as a critical structural element in the conformational activation of αI integrinsRegulation of integrin affinity on cell surfacesTransmigration of neutrophils across inflamed endothelium is signaled through LFA-1 and Src family kinase.Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo.The regulation of integrin function by divalent cations.The connection between metal ion affinity and ligand affinity in integrin I domainsDynamic structural changes are observed upon collagen and metal ion binding to the integrin α1 I domain.Isoflurane binds and stabilizes a closed conformation of the leukocyte function-associated antigen-1.Impact of mutations on the allosteric conformational equilibrium.Activation of integrin beta-subunit I-like domains by one-turn C-terminal alpha-helix deletionsStructure and mechanics of integrin-based cell adhesion.Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring.Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU
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P2860
NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
NMR and mutagenesis evidence f ...... ated antigen 1 ligand binding.
@en
type
label
NMR and mutagenesis evidence f ...... ated antigen 1 ligand binding.
@en
prefLabel
NMR and mutagenesis evidence f ...... ated antigen 1 ligand binding.
@en
P2093
P2860
P356
P1476
NMR and mutagenesis evidence f ...... ated antigen 1 ligand binding.
@en
P2093
Lupher ML Jr
Olejniczak ET
Staunton DE
P2860
P304
P356
10.1073/PNAS.97.10.5231
P407
P577
2000-05-01T00:00:00Z