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Biomedical Research

Volume 29

Page 23

Note:

allied

academies

CARDIOLOGY AND CARDIOVASCULAR MEDICINE

STEM CELLS AND REGENERATIVE MEDICINE

International Conference on

J u n e 1 8 - 1 9 , 2 0 1 8 | O s a k a , J a p a n

Joint Event on

STUDY ON MOLECULAR MECHANISM

OF VASCULAR SMOOTH MUSCLE

RELAXATION BY INCORPORATING THE

WENXIANG DIAGRAM INTO THE NMR

Guo-Ping Zhou

Guangxi Academy of Sciences, China

hysiologic relaxation of vascular smooth muscle is induced by the

cyclic guanosine monophosphate (cGMP)-dependent protein kinase

Iα enzyme (cGKIα), which activates myosin phosphatase (MLCP). This

activation process is thought to occur through the interaction involving

both N- and C-terminal leucine zipper coiled-coil (LZCC) domains of

the kinase enzyme (cGKIα) with the myosin binding subunit (MBS) of

MLCP. In this study, we summarize how to define the LZCC domains in

both N-terminal cGKI

1-59

and C-terminal MBS proteins using predictive

and experimental methods, how to make a rapid and accurate structure

determination of a cGKI

1-59

molecule using NMR’s residual dipolar

coupling (RDC) measurements, and how to indentify the existence of a

weak protein interaction between N-terminal LZCC domain (cGKI1-59)

and a LZCC domain (MBSCT42) within the C-terminal MBS. In addition,

the location and orientation of the residues in LZCC proteins can be readily

visualized using a novel diagram, the so-called “wenxiang diagram”,

which is more advantageous than traditional helical wheel diagrams in

analyzing LZCC protein structures and their action mechanisms. Using

the composed Wenxiang diagrams, we have characterized the interaction

between cGKIα1-59 and another LZCC molecule (MBSCT42), and

deduced that the most affected residues of these two LZCC molecules

might be at the positions d, a, e and g. It is intriguing to see that the

successful incorporation of Wenxiang diagrams and NMR spectroscopy

in the LZCC structural and functional studies may provide some insights

into molecular mechanism of vascular smooth muscle relaxation and

contraction.

Guo-Ping Zhou is a current Professor of Gordon

Life Science Institute, USA. He is also an Adjunct

Professor of several academics in both USA and

China. He received his PhD in Biophysics from

University of California at Davis, and completed

his postdoctoral training at Stanford Universi-

ty and Harvard University, respectively. He has

determined the 3D NMR structures of some

important biomolecules, and successfully intro-

duced the novel diagram approach to elucidate

the mechanisms of the protein-biomolecule

interactions, and protein misfolding diseases

observed by NMR spectroscopy. His current re-

search is focused on the molecular mechanism

of Neural Cell Adhesion Molecule polysialylation

using NMR and biophysical approaches. In ad-

dition, he has also edited some special issues

on the fields of structural biology and medicinal

chemistry for several influential scientific jour-

nals as an Editorial-Board Member and Guest

Editor.

gpzhou@gordonlifescience.org

BIOGRAPHY

Guo-Ping Zhou, Biomed Res 2018, Volume 29 | DOI: 10.4066/biomedicalresearch-C2-005