MORE ABOUT HKUST
University News
Academic Departments A-Z
Life@HKUST
Library
Map & Directions
Jobs@HKUST
Faculty Profiles
About HKUST

Search

More About HKUST
Home Why LIFS? Careers Contact Us
HKUST HKUST Division of Life Science
Research
FacultyResearch AreasFacilities
Education
Undergraduate
ProgramsScholarshipsCurriculumAdmissionCoursesResearch ProjectsInternshipsUndergraduate Advising TeamArticulation Pathways
Postgraduate
MPhil/PhD in Life SciencePhD Dual-degree ProgrammeMSc in BiotechnologyAdmissionCoursesSummer Camp
QA at HKUST
News & Events
NewsEvents
Home
September 21, 2019 by LIFS Editor News 0 comments

Target binding mechanisms governing the WW domain-containing proteins decoded

Prof. Mingjie Zhang and his collaborators decoded the binding mechanisms governing the WW domain tandem-containing proteins. Their findings, published in eLife, reveal the recognition mechanisms of tandem WW domains with their peptide ligands which can serve as a guiding tool for functional studies of WW domain-containing proteins in the future.

WW domain is one of the smallest protein-protein interaction domains composed of only ~35 amino acid residues and widely distributed in many proteins with diverse functions. The PY motif-containing ligands are one of the known targets of WW tandem proteins and are involved in the Hippo signaling pathway responsible for cell adhesion and cell growth. However, the low-affinity interaction of WW/PY-motif has caused difficulties in discriminating among potential PY motif-containing ligands. 

In this study, the team determined the high-resolution structures of 7 representative WW tandem/target complexes and systematically compared the binding affinity of more than 100 WW domain tandems or isolated WW domains binding to previously known or unknown targets. They discovered that WW tandem has strong and specific interactions with PY-motif-containing ligands after a specific structural arrangement of tandem WW domains. Searching this relaxed, extended motif throughout the human proteome led to the identification of novel high-affinity binders to MAGI3 (membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3) and KIBRA (kidney and brain expressed protein).

The novel interaction mechanism has a major impact on the WW domain protein interaction networks and understanding these structural relationships will provide insights on some of the questions in cell growth and polarity regulatory protein networks where numerous WW domains are involved.

Journal Reference:

Lin Z, Yang Z, Xie R, Ji Z, Guan K, Zhang M. Decoding WW domain tandem-mediated target recognitions in tissue growth and cell polarity. Elife. 2019 Sep 5;8:e49439. doi: 10.7554/eLife.49439

 

cell growth cell polarity publication research structural biology WW domain
1

Related Posts

International Human Epigenome Consortium

August 16, 2018
Read More

George K Lee Foundation Scholarships 2018/19 winners announced

June 14, 2019
Read More

GAS2L1 phosphorylation mediated by Nek2 induces centrosome disjunction during cell cycle

February 8, 2021
Read More

Scientists reveal the molecular mechanism of Microprocessor in Caenorhabditis elegans

January 31, 2023
Read More

LIFS researchers reveal mechanism governing AMPAR synaptic targeting and clusteringPrevious Post
Pathogenesis of Usher syndrome, a hereditary deafness diseaseNext Post

ADDRESS

Division of Life Science
The Hong Kong University of Science and Technology
Clear Water Bay
Kowloon, Hong Kong

PHONE

Facsimile No. :
(852) 2358 1552

Telephone No. :
(852) 2358-7272 / 7339
  • Home
  • Careers
  • Contact us
  • Faculty
  • Intranet
HKUST
PrivacySitemap
Copyright © The Hong Kong University of Science and Technology.All rights reserved.
Follow HKUST on
FacebookInstagramLinkedinYouTube
PrivacySitemap