WW domains and retrovirus budding

Article Abstract:

The Yes-associated protein (Yap), containing a WW motif, may be responsible for the concluding budding stages for Rous sarcoma virus (RSV). Research on retroviral Gag proteins' interface with the host cell reveals Yap's interaction with the L domain of RSV in living organisms. The L sequences of RSV, human immunodeficiency virus and equine infectious anaemia virus are distinct giving rise to the possibility of three host proteins, not all containing WW, in the late stages of RSV budding. Filter-binding assays show WW's good binding with the L sequence of the RSV.

Research, Reports, Observations, Retroviruses, Budding, Grafting (Horticulture), Rous sarcoma

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Structure of the WW domain of a kinase-associated protein complexed with-a proline-rich peptide

Article Abstract:

The WW domain of a human Yes kinase-associated protein in proline-rich peptide complex with the bound peptide GTPPPPYTVG is a slightly curved, 3-stranded, antiparallel beta-sheet. This solution structure includes two prolines that are present next to the first tryptophan, and form a hydrophobic buckle on the convex side of the sheet. The concave side comprises three hydrophobic residues which are binding sites for the ligand. A non-conserved isoleucine in the region of amino-terminal flanking covers the exposed hydrophobic residues and stabilizes the WW domain.

Analysis, Physiological aspects, Peptides, Protein kinases

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Crystal structure of a Src-homology 3 (SH3) domain

Article Abstract:

The three-dimensional structure of the Src-homologous SH3 domain of the cytoskeletal protein spectrin has been determined at the 1.8 angstrom level. Spectrin is important because it is the principal constituent of the cytoskeleton supporting the cell membrane. The domain is arranged as a beta-barrel consisting of five antiparallel beta-strands. This structure, with its unusual conserved residues of SH3 genetic sequences, probably functions as a binding site for the protein ligand.

Composition, Cytoskeleton

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