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Articles by Stuart A MacGowan
Structural extension of the human exocyst is enabled by a minimal interface
Abstract In multicellular organisms, the machinery responsible for polarized trafficking directs constitutive cargo secretion at distinct sites of the plasma membrane, cilia, and junctional structures. Central to this machinery is the exocyst complex, which tethers cargo vesicles to their destination membrane, alongside other intracellular membrane tethering roles. Precisely how the exocyst spatially integrates membranes and membrane resident binding partners is unclear.
A unified analysis of evolutionary and population constraint in protein domains highlights structural features and pathogenic sites - Communications Biology
Abstract Protein evolution is constrained by structure and function, creating patterns in residue conservation that are routinely exploited to predict structure and other features. Similar constraints should affect variation across individuals, but it is only with the growth of human population sequencing that this has been tested at scale. Now, human population constraint has established applications in pathogenicity prediction, but it has not yet been explored for structural inference.
Classification of likely functional class for ligand binding sites identified from fragment screening - Communications Biology
Abstract Fragment screening is used to identify binding sites and leads in drug discovery, but it is often unclear which binding sites are functionally important. Here, data from 37 experiments, and 1309 protein structures binding to 1601 ligands were analysed. A method to group ligands by binding sites is introduced and sites clustered according to profiles of relative solvent accessibility. This identified 293 unique ligand binding sites, grouped into four clusters (C1-4).
Missense variants in human ACE2 strongly affect binding to SARS-CoV-2 Spike providing a mechanism for ACE2 mediated genetic risk in Covid-19: A case study in affinity predictions of interface variants
Dear Prof Barton, Thank you very much for submitting your manuscript "Missense variants in human ACE2 strongly affect binding to SARS-CoV-2 Spike providing a mechanism for ACE2 mediated genetic risk and protection from Covid-19" (PCOMPBIOL-D-21-01630R1) for consideration at PLOS Computational Biology. As with all papers peer reviewed by the journal, your manuscript was reviewed by members of the editorial board and by several independent peer reviewers.
Effects of common mutations in the SARS-CoV-2 Spike RBD and its ligand, the human ACE2 receptor on binding affinity and kinetics
Abstract The interaction between the SARS-CoV-2 virus Spike protein receptor binding domain (RBD) and the ACE2 cell surface protein is required for viral infection of cells. Mutations in the RBD are present in SARS-CoV-2 variants of concern that have emerged independently worldwide. For example, the B.1.1.7 lineage has a mutation (N501Y) in its Spike RBD that enhances binding to ACE2. There are also ACE2 alleles in humans with mutations in the RBD binding site.
Human Missense Variation is Constrained by Domain Structure and Highlights Functional and Pathogenic Residues
AbstractHuman genome sequencing has generated population variant datasets containing millions of variants from hundreds of thousands of individuals [1-3]. The datasets show the genomic distribution of genetic variation to be influenced on genic and sub-genic scales by gene essentiality, [1,4,5] protein domain architecture [6] and the presence of genomic features such as splice donor/acceptor sites.
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