1el0
From Proteopedia
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| - | [[Image:1el0.gif|left|200px]] | + | [[Image:1el0.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309''' | + | {{Structure |
| + | |PDB= 1el0 |SIZE=350|CAPTION= <scene name='initialview01'>1el0</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EL0 is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10821677 10821677] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clark-Lewis, I.]] | [[Category: Clark-Lewis, I.]] | ||
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[[Category: chemokine fold]] | [[Category: chemokine fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:57:04 2008'' |
Revision as of 08:57, 20 March 2008
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SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Asthma, susceptibility to OMIM:[601156], HIV1, resistance to OMIM:[601156]
About this Structure
1EL0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
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