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Volume 10, Issue 8 (Suppl)

J Proteomics Bioinform, an open access journal

ISSN: 0974-276X

Structural Biology 2017

September 18-20, 2017

International Conference on

Structural Biology

September 18-20, 2017 Zurich, Switzerland

Brian Kloss, J Proteomics Bioinform 2017, 10:8(Suppl)

DOI: 10.4172/0974-276X-C1-0100

Structural genomics of integral membrane proteins - Past successes and future directions

Brian Kloss

New York Structural Biology, USA

pproximately one-third of all human genes, as well as genes from most other organisms, across all kingdoms of life -

encode integral membrane proteins. Nonetheless, the number of integral membrane protein structures solved lags far

behind the number of those solved for their soluble counterparts, due primarily to the difficulty of recombinant expression

and the instability of membrane proteins once they are detergent-extracted from the lipid bilayer. Over the past 10-20 years,

the number of integral membrane protein structures solved, primarily by x-ray crystallography, has increased significantly

and structural genomics approaches have played a considerable role in this progress. More recently, advances in cryo-electron

microscopy techniques have permitted structures of integral membrane proteins to be determined at resolutions comparable

to that of x-ray crystallography, but requiring much smaller quantities of protein. Concurrently, detergents that improve the

stability of integral membrane proteins and purification techniques that allow proteins to be extracted and purified in their

native lipid environment have also been developed, allowing structural studies of integral membrane proteins to move forward

at an exceedingly rapid pace. I will summarize our past integral membrane protein structural biology efforts that employed

structural genomics approaches and high-throughput techniques and describe our plans for future structural studies that will

continue to make use genomics-based methods, as well as more recently available reagents, techniques and technologies.

Biography

Brian Kloss began his research career as a graduate student in the Laboratory of Carter Bancroft at the Mount Sinai School of Medicine, studying the transcriptional

regulation of the pituitary-specific prolactin and growth hormone genes. He went on to do a Postdoc with Michael Young at Rockefeller University, studying the

genetic control of circadian rhythms in

Drosophila melanogaster

. Afterwards, he spent almost six years at a biotech startup, helping to develop a cell-based assay

for the screening of ligands of GPCRs. For the past ten years, he has been a part of the protein production facility of the Center on Membrane Protein Production

and Analysis (COMPPÅ), located at the New York Structural Biology Center. There, he has led a small group focused on the identification, cloning and expression

screening of integral membrane proteins of prokaryotic origin, mainly for structural studies.

bkloss@nysbc.org

Figure1:

Ribbon diagram showing the structure

of the homologue of the human calcium-activated

chloride channel bestrophin from Klebsiella

pneumoniae.