J
Jia-huai Wang
Researcher at Harvard University
Publications - 115
Citations - 9353
Jia-huai Wang is an academic researcher from Harvard University. The author has contributed to research in topics: T-cell receptor & Integrin. The author has an hindex of 48, co-authored 107 publications receiving 8791 citations. Previous affiliations of Jia-huai Wang include Dana Corporation & Howard Hughes Medical Institute.
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Journal ArticleDOI
Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
TL;DR: The atomic basis for allosteric regulation of the conformation and affinity for ligand of the integrin ectodomain is defined, and how fibrinogen-mimetic therapeutics bind to platelet integrin αIIbβ3 is defined.
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Atomic structure of a thermostable subdomain of HIV-1 gp41.
TL;DR: This thermostable subdomain displays the salient features of the core structure of the isolated gp41 subunit and thus provides a possible target for therapeutics designed selectively to block HIV-1 entry.
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Atomic structure of a fragment of human cd4 containing two immunoglobulin-like domains
Jia-huai Wang,Youwei Yan,Youwei Yan,Thomas P. J. Garrett,Thomas P. J. Garrett,Jin-huan Liu,David W. Rodgers,Robert L. Garlick,George E. Tarr,Yasmin Husain,Ellis L. Reinherz,Stephen C. Harrison,Stephen C. Harrison +12 more
TL;DR: The structure of an N-terminal fragment of CD4 has been determined to 2.4 Å resolution and the binding sites for monoclonal antibodies, class II major histocom-patibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.
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Structures of the αL I Domain and Its Complex with ICAM-1 Reveal a Shape-Shifting Pathway for Integrin Regulation
Motomu Shimaoka,Tsan Sam Xiao,Jin Huan Liu,Yuting Yang,Yicheng Dong,Chang-Duk Jun,Alison McCormack,Rongguang Zhang,Andrzej Joachimiak,Junichi Takagi,Jia-huai Wang,Timothy A. Springer +11 more
TL;DR: Liganded and unliganded structures for both high- and intermediate-affinity mutant I domains reveal that ligand binding can induce conformational change in the alpha L I domain and that allosteric signals can convert the closed conformation to intermediate or open conformations without ligandbinding.
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The crystal structure of a T cell receptor in complex with peptide and MHC class II
Ellis L. Reinherz,Kemin Tan,Lei Tang,Petra Kern,Jin-huan Liu,Yi Xiong,Rebecca E. Hussey,Alex Smolyar,Brian Hare,Rongguang Zhang,Andrzej Joachimiak,Hsiu-Ching Chang,Gerhard Wagner,Jia-huai Wang +13 more
TL;DR: That docking is limited to one segment of MHC-bound peptide offers an explanation for epitope recognition and altered peptide ligand effects, suggests a structural basis for alloreactivity, and illustrates how bacterial superantigens can span the TCR-pMHCII surface.