1lot
From Proteopedia
(New page: 200px<br /> <applet load="1lot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lot, resolution 2.50Å" /> '''CRYSTAL STRUCTURE O...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lot.gif|left|200px]]<br /> | + | [[Image:1lot.gif|left|200px]]<br /><applet load="1lot" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lot" size=" | + | |
caption="1lot, resolution 2.50Å" /> | caption="1lot, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A high-affinity complex formed between G-actin and plasma vitamin | + | A high-affinity complex formed between G-actin and plasma vitamin D-binding protein (DBP) is believed to form part of a scavenging system in the plasma for removing actin released from damaged cells. In the study presented here, we describe the crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution. The complex contains one molecule of each protein bound together by extensive ionic, polar, and hydrophobic interactions. It includes an ATP and a calcium ion bound to actin, but no evidence of vitamin D metabolites bound to the DBP. Both actin and DBP are multidomain molecules, two major domains in actin and three in DBP. All of these domains contribute to the interaction between the molecules. DBP enfolds the end of the actin molecule, principally in actin subdomain 3 but with additional interactions in actin subdomain 1. This orientation is similar to the binding of profilin to actin, as predicted from previous studies. The more extensive interactions of DBP give an affinity for actin some 3 orders of magnitude higher than that for profilin. The larger "footprint" of DBP on actin also leads to an overlap with the actin-binding site of gelsolin domain I. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LOT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with CA, ATP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LOT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOT OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Head, J | + | [[Category: Head, J F.]] |
[[Category: Ray, R.]] | [[Category: Ray, R.]] | ||
[[Category: Swamy, N.]] | [[Category: Swamy, N.]] | ||
| Line 27: | Line 26: | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:57 2008'' |
Revision as of 11:46, 21 February 2008
|
CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN
Contents |
Overview
A high-affinity complex formed between G-actin and plasma vitamin D-binding protein (DBP) is believed to form part of a scavenging system in the plasma for removing actin released from damaged cells. In the study presented here, we describe the crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution. The complex contains one molecule of each protein bound together by extensive ionic, polar, and hydrophobic interactions. It includes an ATP and a calcium ion bound to actin, but no evidence of vitamin D metabolites bound to the DBP. Both actin and DBP are multidomain molecules, two major domains in actin and three in DBP. All of these domains contribute to the interaction between the molecules. DBP enfolds the end of the actin molecule, principally in actin subdomain 3 but with additional interactions in actin subdomain 1. This orientation is similar to the binding of profilin to actin, as predicted from previous studies. The more extensive interactions of DBP give an affinity for actin some 3 orders of magnitude higher than that for profilin. The larger "footprint" of DBP on actin also leads to an overlap with the actin-binding site of gelsolin domain I.
Disease
Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[139200]
About this Structure
1LOT is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution., Head JF, Swamy N, Ray R, Biochemistry. 2002 Jul 23;41(29):9015-20. PMID:12119014
Page seeded by OCA on Thu Feb 21 13:46:57 2008
Categories: Homo sapiens | Oryctolagus cuniculus | Protein complex | Head, J F. | Ray, R. | Swamy, N. | ATP | CA | GOL | Structural protein | Transport protein
