1hxn
From Proteopedia
(New page: 200px<br /><applet load="1hxn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hxn, resolution 1.8Å" /> '''1.8 ANGSTROMS CRYSTAL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hxn.gif|left|200px]]<br /><applet load="1hxn" size=" | + | [[Image:1hxn.gif|left|200px]]<br /><applet load="1hxn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hxn, resolution 1.8Å" /> | caption="1hxn, resolution 1.8Å" /> | ||
'''1.8 ANGSTROMS CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN'''<br /> | '''1.8 ANGSTROMS CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Haemopexin is a serum glycoprotein that binds haem reversibly | + | BACKGROUND: Haemopexin is a serum glycoprotein that binds haem reversibly and delivers it to the liver where it is taken up by receptor-mediated endocytosis. Haemopexin has two homologous domains, each having a characteristic fourfold internal sequence repeat. Haemopexin-type domains are also found in other proteins, including the serum adhesion protein vitronectin and various collagenases, in which they mediate protein-protein interactions. RESULTS: We have determined the crystal structure of the C-terminal domain of haemopexin at 1.8 A resolution. The domain is folded into four beta-leaflet modules, arranged in succession around a central pseudo-fourfold axis. A funnel-shaped tunnel through the centre of this disc-shaped domain serves as an ion-binding site. CONCLUSIONS: A model for haem binding by haemopexin is proposed, utilizing an anion-binding site at the wider end of the central tunnel, together with an associated cleft. This parallels the active-site location in other beta-propeller structures. The capacity to bind both cations and anions, together with the disc shape of the domain, suggests that such domains may be used widely for macromolecular recognition. |
==About this Structure== | ==About this Structure== | ||
| - | 1HXN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PO4, NA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HXN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXN OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, E | + | [[Category: Baker, E N.]] |
| - | [[Category: Faber, H | + | [[Category: Faber, H R.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: NA]] | [[Category: NA]] | ||
| Line 20: | Line 20: | ||
[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:54 2008'' |
Revision as of 11:05, 21 February 2008
|
1.8 ANGSTROMS CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN
Overview
BACKGROUND: Haemopexin is a serum glycoprotein that binds haem reversibly and delivers it to the liver where it is taken up by receptor-mediated endocytosis. Haemopexin has two homologous domains, each having a characteristic fourfold internal sequence repeat. Haemopexin-type domains are also found in other proteins, including the serum adhesion protein vitronectin and various collagenases, in which they mediate protein-protein interactions. RESULTS: We have determined the crystal structure of the C-terminal domain of haemopexin at 1.8 A resolution. The domain is folded into four beta-leaflet modules, arranged in succession around a central pseudo-fourfold axis. A funnel-shaped tunnel through the centre of this disc-shaped domain serves as an ion-binding site. CONCLUSIONS: A model for haem binding by haemopexin is proposed, utilizing an anion-binding site at the wider end of the central tunnel, together with an associated cleft. This parallels the active-site location in other beta-propeller structures. The capacity to bind both cations and anions, together with the disc shape of the domain, suggests that such domains may be used widely for macromolecular recognition.
About this Structure
1HXN is a Single protein structure of sequence from Oryctolagus cuniculus with , and as ligands. Full crystallographic information is available from OCA.
Reference
1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin., Faber HR, Groom CR, Baker HM, Morgan WT, Smith A, Baker EN, Structure. 1995 Jun 15;3(6):551-9. PMID:8590016
Page seeded by OCA on Thu Feb 21 13:05:54 2008
Categories: Oryctolagus cuniculus | Single protein | Baker, E N. | Faber, H R. | CL | NA | PO4 | Heme
