1el0: Difference between revisions

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[[Image:1el0.gif|left|200px]]
[[Image:1el0.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1el0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el0 OCA], [http://www.ebi.ac.uk/pdbsum/1el0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1el0 RCSB]</span>
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'''SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309'''
'''SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309'''
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==About this Structure==
==About this Structure==
1EL0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EL0 OCA].  
1EL0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EL0 OCA].  


==Reference==
==Reference==
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[[Category: Slupsky, C M.]]
[[Category: Slupsky, C M.]]
[[Category: Sykes, B D.]]
[[Category: Sykes, B D.]]
[[Category: chemokine fold]]
[[Category: Chemokine fold]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:04:42 2008''

Revision as of 15:13, 2 May 2008

File:1el0.gif

Template:STRUCTURE 1el0

SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309


OverviewOverview

I-309 is a member of the CC subclass of chemokines and is one of only three human chemokines known to contain an additional, third disulfide bond. The three-dimensional solution structure of I-309 was determined by (1)H nuclear magnetic resonance spectroscopy and dynamic simulated annealing. The structure of I-309, which remains monomeric at high concentrations, was determined on the basis of 978 experimental restraints. The N-terminal region of I-309 was disordered, as has been previously observed for the CC chemokine eotaxin but not others such as MCP-1 and RANTES. This was followed in I-309 by a well-ordered region between residues 13 and 69 that consisted of a 3(10)-helix, a triple-stranded antiparallel beta-sheet, and finally a C-terminal alpha-helix. Root-mean-square deviations of 0.61 and 1.16 were observed for the backbone and heavy atoms, respectively. A comparison of I-309 to eotaxin and HCC-2 revealed a significant structural change in the C-terminal region of the protein. The alpha-helix normally present in chemokines was terminated early and was followed by a short section of extended strand. These changes were a direct result of the additional disulfide bond present in this protein. An examination of the I-309 structure will aid in an understanding of the specificity of this protein with its receptor, CCR8.

About this StructureAbout this Structure

1EL0 is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Human CC chemokine I-309, structural consequences of the additional disulfide bond., Keizer DW, Crump MP, Lee TW, Slupsky CM, Clark-Lewis I, Sykes BD, Biochemistry. 2000 May 23;39(20):6053-9. PMID:10821677 Page seeded by OCA on Fri May 2 15:13:48 2008

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