Left-handed polyproline II helices commonly occur in globular proteins.
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Crystal structure of LIR-2 (ILT4) at 1.8 A: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18.Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding proteinAtypical polyproline recognition by the CMS N-terminal Src homology 3 domainMolecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASPThe synaptic acetylcholinesterase tetramer assembles around a polyproline II helixPex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptorThe structure and function of proline-rich regions in proteinsThe PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activityAssociation of the vav proto-oncogene product with poly(rC)-specific RNA-binding proteinsConservation of the Escherichia coli dnaX programmed ribosomal frameshift signal in Salmonella typhimuriumPhosphopeptide interactions with BRCA1 BRCT domains: More than just a motifAssignment of PolyProline II conformation and analysis of sequence--structure relationshipModel peptide studies of sequence regions in the elastomeric biomineralization protein, Lustrin A. I. The C-domain consensus-PG-, -NVNCT-motifThe structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice modelNMR Solution Structure of the Neurotrypsin Kringle Domain † ‡Identification, structure, and functional requirement of the Mediator submodule Med7N/31NMR studies of the solution conformation of the sex peptide from Drosophila melanogasterCombining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJCrystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucoseWW and SH3 domains, two different scaffolds to recognize proline-rich ligandsThe SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15RKnowledge-Based Protein ModelingRole of the α Clamp in the Protein Translocation Mechanism of Anthrax ToxinThe IDL of E. coli SSB links ssDNA and protein binding by mediating protein-protein interactions.The tale of SSBSynthesis and evaluation of a (3R,6S,9S)-2-oxo-1-azabicyclo[4.3.0]nonane scaffold as a mimic of Xaa-trans-Pro in poly-L-proline type II helix conformation.Purification and reconstitution of the connexin43 carboxyl terminus attached to the 4th transmembrane domain in detergent micellesStructural basis of Robo proline-rich motif recognition by the srGAP1 Src homology 3 domain in the Slit-Robo signaling pathway.The distribution and function of alternatively spliced insertions in hDlg.Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p.Refined solution structure and backbone dynamics of HIV-1 Nef.Involvement of a polyproline helix-like structure in the interaction of 7B2 with prohormone convertase 2.Regulation of the Src protein tyrosine kinase.Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos.Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs.Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition.Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean.Novel methods for secondary structure determination using low wavelength (VUV) circular dichroism spectroscopic data.IMPIPS: the immune protection-inducing protein structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine developmentOn the occurrence of linear groups in proteins.
P2860
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P2860
Left-handed polyproline II helices commonly occur in globular proteins.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
Left-handed polyproline II helices commonly occur in globular proteins.
@en
Left-handed polyproline II helices commonly occur in globular proteins.
@nl
type
label
Left-handed polyproline II helices commonly occur in globular proteins.
@en
Left-handed polyproline II helices commonly occur in globular proteins.
@nl
prefLabel
Left-handed polyproline II helices commonly occur in globular proteins.
@en
Left-handed polyproline II helices commonly occur in globular proteins.
@nl
P356
P1476
Left-handed polyproline II helices commonly occur in globular proteins.
@en
P2093
Adzhubei AA
Sternberg MJ
P304
P356
10.1006/JMBI.1993.1047
P407
P577
1993-01-01T00:00:00Z