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VHL (von Hippel-Lindau) is a tumor suppressor that is associated with von Hippel-Lindau syndrome.  This syndrome is characterized by the predispostion to develop renal tumors in particular, but also tumors of the central nervous system, retina, pancreas and adrenal gland.  The syndrome develops with a germline mutation of VHL, and tumorigenesis occurs when the wild-type allele is mutated.  VHL is found in a complex with ElonginC and ElonginB. The entire complex is called the VCB complex. ElonginB does not interact with VHL directly, so the focus will be only on the interactions between ElonginC and VHL.

Stebbins, C.E., Kaelin, W.G., Pavletich, N.P. Science 284 (1999),455-460.
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Shown in yellow is VHL.  VHL has two domains: a beta domain and an alpha domain.  
The beta domain consists of a seven-stranded beta sandwich and an alpha helix (shown in blue).  The alpha helix interacts directly with the beta sheets through hydrophobic interactions.  
The alpha domain consists of three alpha helices that form a four-helix cluster when bound to Elongin C.  Elongin C provides the fourth helix (shown later).  
The alpha and beta domains are connected by two short polypeptide linkers and by hydrogen bonds between the gold helix, the beta sandwich and Elongin C.
 There is a well-conserved region of 12 amino acids located in the H1 helix (gold).  It is in this region that roughly 25% of the tumor-derived mutations occur.

Stebbins, C.E., Kaelin, W.G., Pavletich, N.P. Science 284 (1999),455-460.
 
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@
 @kinemage 2
@caption
Shown in this image is Elongin C.  Elongin C is highly conserved between eukaryotes. It is involved in several mammalian complexes, but its function is unclear. It is clear, however, that Elongin C plays an important role in the VCB complex by stabilizing VHL through protein-protein interactions.
 Elongin C consists of a three-stranded beta sheet and four helices.  The C-terminal helix is separated by a long, well-ordered loop.  The extended loop together with two helices from VHL and the H4 (green) helix of Elongin C form a pocket that is important in VHL binding.


Stebbins, C.E., Kaelin, W.G., Pavletich, N.P. Science 284 (1999),455-460.

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