1ce7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ce7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ce7, resolution 2.7&Aring;" /> '''MISTLETOE LECTIN I FR...)
Line 1: Line 1:
-
[[Image:1ce7.gif|left|200px]]<br /><applet load="1ce7" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ce7.gif|left|200px]]<br /><applet load="1ce7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ce7, resolution 2.7&Aring;" />
caption="1ce7, resolution 2.7&Aring;" />
'''MISTLETOE LECTIN I FROM VISCUM ALBUM'''<br />
'''MISTLETOE LECTIN I FROM VISCUM ALBUM'''<br />
==Overview==
==Overview==
-
The crystal structure of the ribosome-inactivating protein (RIP) mistletoe, lectin I (ML-I) from Viscum album has been solved by molecular replacement, techniques. The structure has been refined to a crystallographic R-factor, of 24.5% using X-ray diffraction data to 2.8 A resolution. The, heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits, RNA-glycosidase activity and a galactose-specific lectin B subunit. The, overall protein fold is similar to that of ricin from Ricinus communis;, however, unlike ricin, ML-I is already medically applied as a component of, a commercially available misteltoe extract with immunostimulating potency, and for the treatment of human cancer. The three-dimensional structure, reported here revealed structural details of this pharmaceutically, important protein. The comparison to the structure of ricin gives more, insights into the functional mechanism of this protein, provides, structural details for further protein engineering studies, and may lead, to the development of more effective therapeutic RIPs.
+
The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album has been solved by molecular replacement techniques. The structure has been refined to a crystallographic R-factor of 24.5% using X-ray diffraction data to 2.8 A resolution. The heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits RNA-glycosidase activity and a galactose-specific lectin B subunit. The overall protein fold is similar to that of ricin from Ricinus communis; however, unlike ricin, ML-I is already medically applied as a component of a commercially available misteltoe extract with immunostimulating potency and for the treatment of human cancer. The three-dimensional structure reported here revealed structural details of this pharmaceutically important protein. The comparison to the structure of ricin gives more insights into the functional mechanism of this protein, provides structural details for further protein engineering studies, and may lead to the development of more effective therapeutic RIPs.
==About this Structure==
==About this Structure==
-
1CE7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viscum_album Viscum album] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CE7 OCA].
+
1CE7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viscum_album Viscum album] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE7 OCA].
==Reference==
==Reference==
Line 22: Line 22:
[[Category: Mikhailov, A.]]
[[Category: Mikhailov, A.]]
[[Category: Perbandt, M.]]
[[Category: Perbandt, M.]]
-
[[Category: Singh, T.P.]]
+
[[Category: Singh, T P.]]
[[Category: Stoeva, S.]]
[[Category: Stoeva, S.]]
[[Category: Voelter, W.]]
[[Category: Voelter, W.]]
Line 29: Line 29:
[[Category: ribosome-inactivating protein type ii]]
[[Category: ribosome-inactivating protein type ii]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:22:42 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:08 2008''

Revision as of 10:05, 21 February 2008


1ce7, resolution 2.7Å

Drag the structure with the mouse to rotate

MISTLETOE LECTIN I FROM VISCUM ALBUM

Overview

The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album has been solved by molecular replacement techniques. The structure has been refined to a crystallographic R-factor of 24.5% using X-ray diffraction data to 2.8 A resolution. The heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits RNA-glycosidase activity and a galactose-specific lectin B subunit. The overall protein fold is similar to that of ricin from Ricinus communis; however, unlike ricin, ML-I is already medically applied as a component of a commercially available misteltoe extract with immunostimulating potency and for the treatment of human cancer. The three-dimensional structure reported here revealed structural details of this pharmaceutically important protein. The comparison to the structure of ricin gives more insights into the functional mechanism of this protein, provides structural details for further protein engineering studies, and may lead to the development of more effective therapeutic RIPs.

About this Structure

1CE7 is a Single protein structure of sequence from Viscum album with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of mistletoe lectin I from Viscum album., Krauspenhaar R, Eschenburg S, Perbandt M, Kornilov V, Konareva N, Mikailova I, Stoeva S, Wacker R, Maier T, Singh T, Mikhailov A, Voelter W, Betzel C, Biochem Biophys Res Commun. 1999 Apr 13;257(2):418-24. PMID:10198229

Page seeded by OCA on Thu Feb 21 12:05:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools