Researchers reveal key human protein's structure, promising new discoveries for leukemia, AIDS and cellular calcium release
As one example, researchers have shown that CD38 interrupts an interaction between the AIDS virus and its point of entry into cells - a protein receptor called CD4. By looking at CD38's 3-D structure, the Cornell researchers identified a peptide, an organic compound composed of amino acids, that they believe may play a role in interrupting the interface between CD4 and HIV-AIDS.
The findings, published in Structure (Vol. 13, Sept. 2005), mark a major step toward designing drugs that could inhibit processes related to certain diseases. Knowing the protein's structure also opens the door to understanding CD38's many functions related to key biological processes about which researchers know very little. It turns out that CD38 helps produce at least two calcium messenger molecules, each of which then opens channels for the release of calcium from specific stores, or reservoirs, within cell organelles.
By revealing CD38's detailed structure, scientists can now begin to examine how the protein's form influences its molecular functions.
Most read news
Other news from the department science
Get the life science industry in your inbox
From now on, don't miss a thing: Our newsletter for biotechnology, pharma and life sciences brings you up to date every Tuesday and Thursday. The latest industry news, product highlights and innovations - compact and easy to understand in your inbox. Researched by us so you don't have to.