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Structure of neurolysin reveals a deep channel that limits substrate access

The zinc metallopeptidase neurolysin is shown by x-ray crystallography to have large structural elements erected over the active site region that allow substrate access only through a deep narrow…
Publisher (opens in a new tab)

Structural basis for agonism and antagonism of hepatocyte growth factor

The crystal structure of NK2 is reported, which forms a “closed” monomeric conformation through interdomain interactions between the N- domain and the second kringle domain (K2) and provides critical insights into the dimerization mechanism that regulates the Met receptor activation by HGF.
NAS (opens in a new tab)

Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern

The structural basis and mode of action for two potent SARS-CoV-2 spike (S)-neutralizing monoclonal antibodies, CV3-1 and CV3-25, are elucidated, which remain effective against emerging variants of concern in vitro and in vivo.
PubMed (opens in a new tab)

Doubling the Size of the Glucocorticoid Receptor Ligand Binding Pocket by Deacylcortivazol

It is reported that the ligand pocket of glucocorticoid receptor (GR) can be continuously extended into the top half of the LBD by binding to deacylcortivazol (DAC), an extremely potent glucoc Corticoid.
Taylor & Francis (opens in a new tab)

Identification of Near-Pan-neutralizing Antibodies against HIV-1 by Deconvolution of Plasma Humoral Responses.

X-ray crystallographic analysis of one monoclonal suggested a unique ability to bypass the CD4bs Phe43 cavity, while reaching deep into highly conserved residues of Layer 3 of the gp120 inner domain, likely explaining its extreme potency and breadth.
PubMed (opens in a new tab)

Co-receptor Binding Site Antibodies Enable CD4-Mimetics to Expose Conserved Anti-cluster A ADCC Epitopes on HIV-1 Envelope Glycoproteins

Test whether small CD4-mimetics able to “push” Env into this conformation sensitize HIV-1-infected cells to ADCC mediated by HIV + sera and results indicate that CD4mc initially open the trimeric Env enough to allow the binding of CoRBS antibodies but not anti-cluster A antibodies.
PubMed (opens in a new tab)

An Asymmetric Opening of HIV-1 Envelope Mediates Antibody-Dependent Cellular Cytotoxicity.

An asymmetric Env conformation (State 2A) is uncovered recognized by antibodies targeting the conserved gp120 inner domain and mediating ADCC, which may represent approaches to fight HIV-1 infection.
PubMed (opens in a new tab)

A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist

The ability to separate the Met-binding activity of NK1 from its Met dimerization activity provides a rational basis for designing Met antagonists and may be applicable for other growth factor receptors by selectively abolishing the receptor activation ability but not the receptor binding of the growth factors.
NAS (opens in a new tab)

The HIV-1 Antisense Protein ASP Is a Transmembrane Protein of the Cell Surface and an Integral Protein of the Viral Envelope

ASP expression in multiple chronically infected myeloid and lymphoid cell lines using an anti-ASP monoclonal antibody and flow cytometry and microscopy approaches indicates that ASP is an integral protein of the plasma membranes of chronically infected cells stimulated with PMA, and upon viral budding, ASP becomes a structuralprotein of the HIV-1 envelope.
Publisher (opens in a new tab)

Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir

The structure-function analysis using engineered viruses and soluble trimer variants reveals that the molecular basis of resistance is mediated by crosstalk between His375 and the inner domain layers, and confirms that temsavir can adjust its binding mode to accommodate changes in Env conformation.
PubMed (opens in a new tab)
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