2hcc

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[[Image:2hcc.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcc OCA], [http://www.ebi.ac.uk/pdbsum/2hcc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hcc RCSB]</span>
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'''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES'''
'''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES'''
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[[Category: Schweimer, K.]]
[[Category: Schweimer, K.]]
[[Category: Sticht, H.]]
[[Category: Sticht, H.]]
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[[Category: cc-chemokine]]
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[[Category: Cc-chemokine]]
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[[Category: chemokine]]
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[[Category: Chemokine]]
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[[Category: chemotaxis]]
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[[Category: Chemotaxis]]
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[[Category: hcc-2]]
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[[Category: Hcc-2]]
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[[Category: human]]
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[[Category: Human]]
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[[Category: leukotactin-1]]
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[[Category: Leukotactin-1]]
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[[Category: mip-5]]
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[[Category: Mip-5]]
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[[Category: nmr structure]]
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[[Category: Nmr structure]]
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Revision as of 03:07, 4 May 2008

Image:2hcc.gif

Template:STRUCTURE 2hcc

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 Sun May 4 06:07:07 2008

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