2qyp: Difference between revisions

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[[Image:2qyp.~~jpg~~|left|200px]]

[[Image:2qyp.png|left|200px]]

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~~'''~~Orthorhombic Crystal Structure of Human Saposin C Dimer in Open Conformation~~'''~~

===Orthorhombic Crystal Structure of Human Saposin C Dimer in Open Conformation===

~~==Overview==~~

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~~Human saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite~~ the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully understood. We describe two crystal structures of human saposin C in an "open" configuration with unusual domain swapped homodimers. This form of SapC dimer supports the ~~"clip-~~on~~" model for SapC-induced vesicle fusion~~. ~~In addition~~, ~~we present~~ the ~~crystal structure of SapD in two crystal forms~~. ~~They reveal the monomer~~-monomer interface for the SapD dimer, which was confirmed in solution by analytical ultracentrifugation. The crystal structure of SapD suggests that side chains of Lys10 and Arg17 are involved in initial association with the preferred anionic biological membranes by forming salt bridges with sulfate or phosphate lipid headgroups.

The line below this paragraph, {{ABSTRACT_PUBMED_18462685}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18462685 is the PubMed ID number.

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==About this Structure==

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[[Category: Saposin]]

[[Category: Sphingolipid metabolism]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu May 22 22~~:29:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:11:00 2008''

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-[[Image:2qyp.jpg|left|200px]]
+{{Seed}}
+[[Image:2qyp.png|left|200px]]
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 {{STRUCTURE_2qyp|  PDB=2qyp  |  SCENE=  }}
-'''Orthorhombic Crystal Structure of Human Saposin C Dimer in Open Conformation'''
+===Orthorhombic Crystal Structure of Human Saposin C Dimer in Open Conformation===
-==Overview==
+<!--
-Human saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully understood. We describe two crystal structures of human saposin C in an "open" configuration with unusual domain swapped homodimers. This form of SapC dimer supports the "clip-on" model for SapC-induced vesicle fusion. In addition, we present the crystal structure of SapD in two crystal forms. They reveal the monomer-monomer interface for the SapD dimer, which was confirmed in solution by analytical ultracentrifugation. The crystal structure of SapD suggests that side chains of Lys10 and Arg17 are involved in initial association with the preferred anionic biological membranes by forming salt bridges with sulfate or phosphate lipid headgroups.
+The line below this paragraph, {{ABSTRACT_PUBMED_18462685}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18462685 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18462685}}
 ==About this Structure==
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 [[Category: Saposin]]
 [[Category: Sphingolipid metabolism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:29:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:11:00 2008''