Abstract:
:CD2 (cluster of differentiation 2) is a cell adhesion molecule expressed on T cells and is recognized as a target for CD48 (rats) and CD58 (humans). Tremendous progress has been achieved in understanding the function of CD2, the mechanism of molecular recognition and protein folding, thus, leading towards the use of this protein as a scaffold for protein design. CD2 has been shown to set quantitative thresholds in T cell activation both in vivo and in vitro. Further, intracellular CD2 signaling pathways and networks are being discovered by the identification of several cytosolic tail binding proteins. In addition, a new method for directly measuring heterophilic adhesion has been developed. The functional "hot spot" for the adhesion surface of CD2 and CD58 has been dissected. Detailed NMR studies reveal that rat CD2 weakly self-associates to form a homodimeric structure in solution. Dynamic interaction of CD2 with the GYF and SH3 domains has been investigated. CD2 has been shown to form fibrils in the presence of 2,2,2-trifluoroethanol (TFE) and at low pH. Furthermore, kinetic studies have been completed to monitor the effect of surface hydrophobic residues and intramolecular bridges on the folding pathways of CD2. Our lab has de novo designed single calcium-binding sites into domain 1 of rat CD2 (CD2-D1) with strong metal selectivity. In addition, the EF-hand motifs have been grafted into CD2 to understand the site-specific calcium-binding affinity of calmodulin and calcium-dependent cell adhesion.
journal_name
Curr Protein Pept Scijournal_title
Current protein & peptide scienceauthors
Wilkins AL,Yang W,Yang JJdoi
10.2174/1389203033487063keywords:
subject
Has Abstractpub_date
2003-10-01 00:00:00pages
367-73issue
5eissn
1389-2037issn
1875-5550journal_volume
4pub_type
杂志文章,评审abstract::Protein-protein interaction (PPI) is necessary for most of the biological processes and requisite for host-pathogen communication. Most of the threatening human diseases are caused by different types of interactions of proteins with their prior infected proteins or with pathogen's proteins. Understanding of involved m...
journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
doi:10.2174/1389203718666170828122927
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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更新日期:2001-03-01 00:00:00
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journal_title:Current protein & peptide science
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abstract::Glucagon-like peptide 2 (GLP-2) is a newly discovered gastrointestinal peptide with 33% sequence homology to glucagon. GLP-2 has attracted interest because of its potent intestinotrophic endocrine/paracrine actions. The peptide, consisting of 33-amino-acid, results from expression of the glucagon gene in the enteroend...
journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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更新日期:2014-01-01 00:00:00
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journal_title:Current protein & peptide science
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