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<Structure load='1g1r' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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== Crystal structure of P-selectin lectin/EGF domains complexed with SLeX ==
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== '''Introduction''' ==
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Selectins are proteins that are include in a family of cell adhesion receptor involved in the diapedese. There are 3 kinds of selectins :
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E selectin localized in endothelial cells,
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L selectin found in leukocytes,
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P selectins in platelets and endothelial cells.
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Diapedese is the movement of leukocytes out of the circulatory system. First, the leukocytes is attracted by cytokines, secreted near the site of infection. Then, this leukocytes slow down and beggin rolling allong the surface of the vessel. He binds then tightly the vessel and immobilizates himself. Finally, he pass through gaps between epithelial cells. By this mecanism, the leukocyte arrives on the site of infection to neutralize the infection agent.
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== '''3D structure''' ==
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== '''References''' ==
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http://cro.sagepub.com/content/10/3/337.full.pdf
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== '''Proteopedia Page Contributors and Editors''' ==
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Delphine Trelat, Cécile Ehrhardt

Revision as of 11:57, 17 December 2012

Template:Sandbox ESBS 2012

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Contents

Crystal structure of P-selectin lectin/EGF domains complexed with SLeX

Introduction

Selectins are proteins that are include in a family of cell adhesion receptor involved in the diapedese. There are 3 kinds of selectins : E selectin localized in endothelial cells, L selectin found in leukocytes, P selectins in platelets and endothelial cells.

Diapedese is the movement of leukocytes out of the circulatory system. First, the leukocytes is attracted by cytokines, secreted near the site of infection. Then, this leukocytes slow down and beggin rolling allong the surface of the vessel. He binds then tightly the vessel and immobilizates himself. Finally, he pass through gaps between epithelial cells. By this mecanism, the leukocyte arrives on the site of infection to neutralize the infection agent.



3D structure

References

http://cro.sagepub.com/content/10/3/337.full.pdf



Proteopedia Page Contributors and Editors

Delphine Trelat, Cécile Ehrhardt

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