1kw2
From Proteopedia
(New page: 200px<br /> <applet load="1kw2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kw2, resolution 2.15Å" /> '''CRYSTAL STRUCTURE O...) |
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caption="1kw2, resolution 2.15Å" /> | caption="1kw2, resolution 2.15Å" /> | ||
'''CRYSTAL STRUCTURE OF UNCOMPLEXED VITAMIN D-BINDING PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF UNCOMPLEXED VITAMIN D-BINDING PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KW2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1KW2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KW2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vitamin d-binding protein]] | [[Category: vitamin d-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:15:23 2008'' |
Revision as of 14:15, 15 February 2008
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CRYSTAL STRUCTURE OF UNCOMPLEXED VITAMIN D-BINDING PROTEIN
Contents |
Overview
Actin is the most abundant protein in eukaryotic cells, but its release, from cells into blood vessels can be lethal, being associated with, clinical situations including hepatic necrosis and septic shock. A, homeostatic mechanism, termed the actin-scavenger system, is responsible, for the depolymerization and removal of actin from the circulation. During, the first phase of this mechanism, gelsolin severs the actin filaments. In, the second phase, the vitamin D-binding protein (DBP) traps the actin, monomers, which accelerates their clearance. We have determined the, crystal structures of DBP by itself and complexed with actin to 2.1 A, resolution. Similar to its homologue serum albumin, DBP consists of three, related domains. Yet, in DBP a strikingly different organization of the, domains gives rise to a large actin-binding cavity. After complex, formation the three domains of DBP move slightly to "clamp" onto actin, subdomain 3 and to a lesser extent subdomain 1. Contacts between actin and, DBP throughout their extensive 3,454-A(2) intermolecular interface involve, a mixture of hydrophobic, electrostatic, and solvent-mediated, interactions. The area of actin covered by DBP within the complex, approximately equals the sum of those covered by gelsolin and profilin., Moreover, certain interactions of DBP with actin mirror those observed in, the actin-gelsolin complex, which may explain how DBP can compete, effectively with gelsolin for actin binding. Formation of the strong, actin-DBP complex proceeds with limited conformational changes to both, proteins, demonstrating how DBP has evolved to become an effective, actin-scavenger protein.
Disease
Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[139200]
About this Structure
1KW2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system., Otterbein LR, Cosio C, Graceffa P, Dominguez R, Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8003-8. Epub 2002 Jun 4. PMID:12048248
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