1hul: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1hul.gif|left|200px]]
{{Seed}}
[[Image:1hul.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hul|  PDB=1hul  |  SCENE=  }}  
{{STRUCTURE_1hul|  PDB=1hul  |  SCENE=  }}  


'''A NOVEL DIMER CONFIGURATION REVEALED BY THE CRYSTAL STRUCTURE AT 2.4 ANGSTROMS RESOLUTION OF HUMAN INTERLEUKIN-5'''
===A NOVEL DIMER CONFIGURATION REVEALED BY THE CRYSTAL STRUCTURE AT 2.4 ANGSTROMS RESOLUTION OF HUMAN INTERLEUKIN-5===




==Overview==
<!--  
Interleukin-5 (IL-5) is a lineage-specific cytokine for eosinophilpoiesis and plays an important part in diseases associated with increased eosinophils, such as asthma. Human IL-5 is a disulphide-linked homodimer with 115 amino-acid residues in each chain. The crystal structure at 2.4 A resolution reveals a novel two-domain structure, with each domain showing a striking similarity to the cytokine fold found in granulocyte macrophage and macrophage colony-stimulating factors, IL-2 (ref. 5), IL-4 (ref. 6), and human and porcine growth hormones. IL-5 is unique in that each domain requires the participation of two chains. The IL-5 structure consists of two left-handed bundles of four helices laid end to end and two short beta-sheets on opposite sides of the molecule. Surprisingly, the C-terminal strand and helix of one chain complete a bundle of four helices and a beta-sheet with the N-terminal three helices and one strand of the other chain. The structure of IL-5 provides a molecular basis for the design of antagonists and agonists that would delineate receptor recognition determinants critical in signal transduction. This structure determination extends the family of the cytokine bundle of four helices and emphasizes its fundamental significance and versatility in recognizing its receptor.
The line below this paragraph, {{ABSTRACT_PUBMED_8483502}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8483502 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8483502}}


==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Milburn, M V.]]
[[Category: Milburn, M V.]]
[[Category: Cytokine]]
[[Category: Cytokine]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:14:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:42:59 2008''

Revision as of 05:43, 1 July 2008

File:1hul.png

Template:STRUCTURE 1hul

A NOVEL DIMER CONFIGURATION REVEALED BY THE CRYSTAL STRUCTURE AT 2.4 ANGSTROMS RESOLUTION OF HUMAN INTERLEUKIN-5

Template:ABSTRACT PUBMED 8483502

About this Structure

1HUL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5., Milburn MV, Hassell AM, Lambert MH, Jordan SR, Proudfoot AE, Graber P, Wells TN, Nature. 1993 May 13;363(6425):172-6. PMID:8483502

Page seeded by OCA on Tue Jul 1 08:42:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1hul&oldid=608818"