From: LARRY KLAES (ljk4_at_msn.com)
Date: Mon Sep 19 2005 - 16:45:09 UTC
>From: cunews_at_cornell.edu
>Reply-To: cunews_at_cornell.edu
>To: CUNEWS-LIFE_SCIENCE-L_at_cornell.edu (CUNEWS-LIFE_SCIENCE-L),
>CUNEWS-SCIENCE-L_at_cornell.edu (CUNEWS-SCIENCE-L)
>Subject: Featuring Cornell: Protein structure
>Date: Mon, 19 Sep 2005 12:20:56 -0400
>
>Researchers reveal key human protein's structure, promising new discoveries
>for leukemia, AIDS and cellular calcium release
>http://www.news.cornell.edu/stories/Sept05/HumanCD38.kr.html
>
>Sept. 19, 2005
>
>By Krishna Ramanujan
>ksr32_at_cornell.edu
>
>
>ITHACA, N.Y. -- Cornell University researchers have discovered the 3-D
>crystal structure of a protein, human CD38, which may lead to important
>discoveries about how cells release calcium -- a mineral used in almost
>every cellular process. The findings also may offer insights into
>mechanisms involved in certain diseases, ranging from leukemia to diabetes
>and HIV-AIDS.
>
>Levels of the protein climb, for reasons unknown, when people fall ill,
>making human CD38 a marker for these diseases.
>
>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 the journal 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.
>
>"For example, the mechanism of how a cell mediates calcium release is
>largely unknown," said the paper's senior author, Quan Hao, director of the
>Macromolecular Diffraction Facility (MacCHESS), the biomedical research arm
>of the Cornell High Energy Synchrotron Source (CHESS). "So this is a very
>fundamental question for biologists."
>
>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.
>
>High intensity X-rays made it possible to pass photons through a protein
>crystal to reveal its structure. Cornell's synchrotron produces beams of
>X-rays millions of times more intense than conventional X-ray generators
>allow. The very intense beams were necessary to determine the atomic
>structure of CD38. The research group, which includes researchers from the
>University of Minnesota, also developed new calculations that allowed them
>to extract the protein's entire structure from the X-ray images.
>
>By revealing CD38's detailed structure, scientists can now begin to examine
>how the protein's form influences its molecular functions.
>
>"People have been struggling with this for a long time, and we have finally
>solved it," said Hao.
>
>The National Institutes of Health, which supports MacCHESS, also funded
>this research. The paper's other lead authors include MacCHESS graduate
>student Qun Liu and researcher support specialist Irina Kriksunov.
>
>-30-
>
>Media Contact: Joe Schwartz
>Phone: (607) 254-6235
>E-mail: bjs54_at_cornell.edu
>
>--
>
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>
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