2c3a: Difference between revisions

Herpes simplex virus (HSV) entry into cells requires binding of the, envelope glycoprotein D (gD) to one of several cell surface receptors. The, 50 C-terminal residues of the gD ectodomain are essential for virus entry, but not for receptor binding. We have determined the structure of an, unliganded gD molecule that includes these C-terminal residues. The, structure reveals that the C-terminus is anchored near the N-terminal, region and masks receptor-binding sites. Locking the C-terminus in the, position observed in the crystals by an intramolecular disulfide bond, abolished receptor binding and virus entry, demonstrating that this region, of gD moves upon receptor binding. Similarly, a point mutant that would, destabilize the C-terminus structure was nonfunctional for entry, despite, increased affinity for receptors. We propose that a controlled, displacement of the gD C-terminus upon receptor binding is an essential, feature of HSV entry, ensuring the timely activation of membrane fusion.

2C3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4] with CL, ZN and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3A OCA].  

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