A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1
نویسندگان
چکیده
منابع مشابه
A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1
Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-indepe...
متن کاملMaltose-binding protein as a solubility enhancer.
1. Introduction A major impediment to the production of recombinant proteins in Escheri-chia coli is their tendency to accumulate in the form of insoluble and biologically inactive aggregates known as inclusion bodies. Although it is sometimes possible to convert aggregated material into native, biologically-active protein , this is a time consuming, labor-intensive, costly, and uncertain under...
متن کاملProkaryotic Soluble Overexpression and Purification of Human VEGF165 by Fusion to a Maltose Binding Protein Tag
Human vascular endothelial growth factor (VEGF) is a key regulator of angiogenesis and plays a central role in the process of tumor growth and metastatic dissemination. Escherichia coli is one of the most common expression systems used for the production of recombinant proteins; however, expression of human VEGF in E. coli has proven difficult because the E. coli-expressed VEGF tends to be misf...
متن کاملMaltose-binding protein is a potential carrier for oral immunizations.
Maltose binding protein (MBP) is often fused to a relevant protein to improve its yield and facilitate its purification, but MBP can also enhance the immunogenicity of the fused proteins. Recent data suggest that MBP may potentiate antigen-presenting functions in immunized animals by providing intrinsic maturation stimuli to dendritic cells through TLR4. The aim of this study was to examine if ...
متن کاملEasy mammalian expression and crystallography of maltose-binding protein-fused human proteins
We present a strategy to obtain milligrams of highly post-translationally modified eukaryotic proteins, transiently expressed in mammalian cells as rigid or cleavable fusions with a mammalianized version of bacterial maltose-binding protein (mMBP). This variant was engineered to combine mutations that enhance MBP solubility and affinity purification, as well as provide crystal-packing interacti...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: PLOS ONE
سال: 2015
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0125010