Mutational analysis of the CD2/CD58 interaction: the binding site for CD58 lies on one face of the first domain of human CD2.
about
A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interactionConformation and function of the N-linked glycan in the adhesion domain of human CD2Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studiesOne sequence, two folds: a metastable structure of CD2Engineering an intertwined form of CD2 for stability and assemblySolution structure of the epithelial cadherin domain responsible for selective cell adhesion.The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC'C" face of the human CD2 adhesion domain.Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1.A genomics approach to the detection of positive selection in cattle: adaptive evolution of the T-cell and natural killer cell-surface protein CD2.Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area.Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains.Processing and localization of the african swine fever virus CD2v transmembrane protein.Amino acid residues required for binding of lymphocyte function-associated antigen 3 (CD58) to its counter-receptor CD2.The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions.CD2 and the nature of protein interactions mediating cell-cell recognition.Costimulatory Function of Cd58/Cd2 Interaction in Adaptive Humoral Immunity in a Zebrafish Model.Ligand Binding by the Immunoglobulin Superfamily Recognition Molecule CD2 Is Glycosylation-independent
P2860
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P2860
Mutational analysis of the CD2/CD58 interaction: the binding site for CD58 lies on one face of the first domain of human CD2.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Mutational analysis of the CD2 ...... the first domain of human CD2.
@en
Mutational analysis of the CD2 ...... the first domain of human CD2.
@nl
type
label
Mutational analysis of the CD2 ...... the first domain of human CD2.
@en
Mutational analysis of the CD2 ...... the first domain of human CD2.
@nl
prefLabel
Mutational analysis of the CD2 ...... the first domain of human CD2.
@en
Mutational analysis of the CD2 ...... the first domain of human CD2.
@nl
P2093
P2860
P356
P1476
Mutational analysis of the CD2 ...... the first domain of human CD2.
@en
P2093
Driscoll PC
Williams AF
P2860
P304
P356
10.1084/JEM.178.2.549
P407
P577
1993-08-01T00:00:00Z