From Proteopedia
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| - | [[Image:1kxp.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1kxp| PDB=1kxp | SCENE= }} | | {{STRUCTURE_1kxp| PDB=1kxp | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN'''
| + | ===CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12048248}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12048248 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12048248}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Dbp]] | | [[Category: Dbp]] |
| | [[Category: Vitamin d-binding protein]] | | [[Category: Vitamin d-binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:17:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:14:36 2008'' |
Revision as of 08:14, 2 July 2008
Template:STRUCTURE 1kxp
CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN
Template:ABSTRACT PUBMED 12048248
About this Structure
1KXP is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. 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
Page seeded by OCA on Wed Jul 2 11:14:36 2008
