2oqp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="2oqp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oqp" /> '''Solution structure of human interleukin-21'...)
Line 1: Line 1:
-
[[Image:2oqp.gif|left|200px]]<br />
+
[[Image:2oqp.jpg|left|200px]]<br /><applet load="2oqp" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="2oqp" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="2oqp" />
caption="2oqp" />
'''Solution structure of human interleukin-21'''<br />
'''Solution structure of human interleukin-21'''<br />
Line 8: Line 7:
==About this Structure==
==About this Structure==
-
2OQP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OQP OCA].
+
2OQP 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=2OQP OCA].
==Reference==
==Reference==
Line 20: Line 19:
[[Category: multiple conformers]]
[[Category: multiple conformers]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:15:08 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:49:40 2008''

Revision as of 10:49, 23 January 2008


2oqp

Drag the structure with the mouse to rotate

Solution structure of human interleukin-21

Overview

The high resolution three-dimensional structure of human interleukin, (hIL)-21 has been resolved by heteronuclear NMR spectroscopy. Overall, the, hIL-21 structure is dominated by a well defined central four-helical, bundle, arranged in an up-up-down-down topology, as observed for other, cytokines. A segment of the hIL-21 molecule that includes the third, helical segment, helix C, is observed to exist in two distinct and, interchangeable states. In one conformer, the helix C segment is presented, in a regular, alpha-helical conformation, whereas in the other conformer, this segment is largely disordered. A structure-based sequence alignment, of hIL-21 with receptor complexes of the related cytokines, interleukin-2, and -4, implied that this particular segment is involved in receptor, binding. An hIL-21 analog was designed to stabilize the region around, helix C through the introduction of a segment grafted from hIL-4. This, novel hIL-21 analog was demonstrated to exhibit a 10-fold increase in, potency in a cellular assay.

About this Structure

2OQP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The existence of multiple conformers of interleukin-21 directs engineering of a superpotent analogue., Bondensgaard K, Breinholt J, Madsen D, Omkvist DH, Kang L, Worsaae A, Becker P, Schiodt CB, Hjorth SA, J Biol Chem. 2007 Aug 10;282(32):23326-36. Epub 2007 Jun 12. PMID:17565991

Page seeded by OCA on Wed Jan 23 12:49:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools