منابع مشابه
Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexes.
Proline-rich sequences (PRS) and their recognition domains have emerged as transposable protein interaction modules during eukaryotic evolution. They are especially abundant in proteins associated with pre-mRNA splicing and likely assist in the formation of the spliceosome by binding to GYF and WW domains. Here we profile PRS-mediated interactions of the CD2BP2/52K GYF domain by a site-specific...
متن کاملHistidine-proline-rich glycoprotein has potent antiangiogenic activity mediated through the histidine-proline-rich domain.
Histidine-proline-rich glycoprotein (HPRG) is an abundant multidomain plasma protein evolutionarily related to high-molecular-weight kininogen. The cleaved form of high-molecular-weight kininogen has recently been demonstrated to exhibit antiangiogenic activities in vitro (J. C. Zhang et al., FASEB J., 14: 2589-2600, 2000), mediated primarily through domain 5. HPRG contains a histidine-proline-...
متن کاملThe unique proline-rich domain of parotid proline-rich proteins functions in secretory sorting.
When expressed in pituitary AtT-20 cells, parotid proline-rich proteins enter the regulated pathway. Because the short N-terminal domain of a basic proline-rich protein is necessary for efficient export from the ER, it has not been possible to evaluate the role of this polypeptide segment as a sorting signal for regulated secretion. We now show that addition of the six-amino acid propeptide of ...
متن کاملBasal and antigen-induced exposure of the proline-rich sequence in CD3ε.
The CD3ε cytoplasmic tail contains a conserved proline-rich sequence (PRS) that influences TCR-CD3 expression and signaling. Although the PRS can bind the SH3.1 domain of the cytosolic adapter Nck, whether the PRS is constitutively available for Nck binding or instead represents a cryptic motif that is exposed via conformational change upon TCR-CD3 engagement (CD3Δc) is currently unresolved. Fu...
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ژورنال
عنوان ژورنال: Molecular & Cellular Proteomics
سال: 2009
ISSN: 1535-9476
DOI: 10.1074/mcp.m800337-mcp200