2hcc
From Proteopedia
(New page: 200px<br /> <applet load="2hcc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hcc" /> '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE H...) |
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| - | [[Image:2hcc.gif|left|200px]]<br /> | + | [[Image:2hcc.gif|left|200px]]<br /><applet load="2hcc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2hcc" size=" | + | |
caption="2hcc" /> | caption="2hcc" /> | ||
'''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce | + | HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce chemotaxis on monocytes, T-lymphocytes, and eosinophils. The three-dimensional structure of HCC-2 has been determined by 1H nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations on the basis of 871 experimental restraints. The structure is well-defined, exhibiting average root-mean-square deviations of 0.58 and 0.96 A for the backbone heavy atoms and all heavy atoms of residues 5-63, respectively. In contrast to most other chemokines, subtle structural differences impede dimer formation of HCC-2 in a concentration range of 0.1 microM to 2 mM. HCC-2, however, exhibits the same structural elements as the other chemokines, i.e., a triple-stranded antiparallel beta-sheet covered by an alpha-helix, showing that the chemokine fold is not influenced by quaternary interactions. Structural investigations with a HCC-2 mutant prove that a third additional disulfide bond present in wild-type HCC-2 is not necessary for maintaining the relative orientation of the helix and the beta-sheet. |
==About this Structure== | ==About this Structure== | ||
| - | 2HCC 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:// | + | 2HCC 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=2HCC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adermann, K.]] | [[Category: Adermann, K.]] | ||
| - | [[Category: Escher, S | + | [[Category: Escher, S E.]] |
| - | [[Category: Forssmann, W | + | [[Category: Forssmann, W G.]] |
[[Category: Roesch, P.]] | [[Category: Roesch, P.]] | ||
[[Category: Schweimer, K.]] | [[Category: Schweimer, K.]] | ||
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[[Category: nmr structure]] | [[Category: nmr structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:26 2008'' |
Revision as of 15:40, 21 February 2008
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SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES
Overview
HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce chemotaxis on monocytes, T-lymphocytes, and eosinophils. The three-dimensional structure of HCC-2 has been determined by 1H nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations on the basis of 871 experimental restraints. The structure is well-defined, exhibiting average root-mean-square deviations of 0.58 and 0.96 A for the backbone heavy atoms and all heavy atoms of residues 5-63, respectively. In contrast to most other chemokines, subtle structural differences impede dimer formation of HCC-2 in a concentration range of 0.1 microM to 2 mM. HCC-2, however, exhibits the same structural elements as the other chemokines, i.e., a triple-stranded antiparallel beta-sheet covered by an alpha-helix, showing that the chemokine fold is not influenced by quaternary interactions. Structural investigations with a HCC-2 mutant prove that a third additional disulfide bond present in wild-type HCC-2 is not necessary for maintaining the relative orientation of the helix and the beta-sheet.
About this Structure
2HCC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype., Sticht H, Escher SE, Schweimer K, Forssmann WG, Rosch P, Adermann K, Biochemistry. 1999 May 11;38(19):5995-6002. PMID:10320325
Page seeded by OCA on Thu Feb 21 17:40:26 2008
Categories: Homo sapiens | Single protein | Adermann, K. | Escher, S E. | Forssmann, W G. | Roesch, P. | Schweimer, K. | Sticht, H. | Cc-chemokine | Chemokine | Chemotaxis | Hcc-2 | Human | Leukotactin-1 | Mip-5 | Nmr structure
