1o8t
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8t OCA], [http://www.ebi.ac.uk/pdbsum/1o8t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o8t RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Apolipoprotein CII (apoCII), a surface constituent of plasma lipoproteins, is the activator for lipoprotein lipase (LPL) and is therefore central for lipid transport in blood. The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported. In addition to the structure determination, (15)N-relaxation measurements have been performed at two magnetic fields to characterize the dynamics of the backbone of apoCII in the complex. The relaxation data also provided global structural constraints, viz. the orientation of helices in the complex. In addition, global constraints were derived from the fact that apoCII helices are attached to the surface of the SDS micelle and that the hydrophobic moments of each helix faces the interior of the micelle. These three categories of global constraints, together with the local classical NMR constraints, were sufficient to define the 3D structure of the apoCII-SDS micelle complex. To our knowledge, this presents the first example in which the global structure of a protein-SDS micelle complex has been determined. The C-terminal helix of apoCII is known to be responsible for the activation of LPL. This helix is distinguished from the other helices by a higher degree of internal motion on the nanosecond time scale as shown by the relaxation data. The overall structure and the internal dynamics, combined with previous mutation data, give important clues toward a possible mechanism for the activation of LPL by apoCII. | Apolipoprotein CII (apoCII), a surface constituent of plasma lipoproteins, is the activator for lipoprotein lipase (LPL) and is therefore central for lipid transport in blood. The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported. In addition to the structure determination, (15)N-relaxation measurements have been performed at two magnetic fields to characterize the dynamics of the backbone of apoCII in the complex. The relaxation data also provided global structural constraints, viz. the orientation of helices in the complex. In addition, global constraints were derived from the fact that apoCII helices are attached to the surface of the SDS micelle and that the hydrophobic moments of each helix faces the interior of the micelle. These three categories of global constraints, together with the local classical NMR constraints, were sufficient to define the 3D structure of the apoCII-SDS micelle complex. To our knowledge, this presents the first example in which the global structure of a protein-SDS micelle complex has been determined. The C-terminal helix of apoCII is known to be responsible for the activation of LPL. This helix is distinguished from the other helices by a higher degree of internal motion on the nanosecond time scale as shown by the relaxation data. The overall structure and the internal dynamics, combined with previous mutation data, give important clues toward a possible mechanism for the activation of LPL by apoCII. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Hyperlipoproteinemia, type Ib OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608083 608083]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: dynamic]] | [[Category: dynamic]] | ||
[[Category: global structure]] | [[Category: global structure]] | ||
| - | [[Category: helix | + | [[Category: helix ,lipid transport,lipid degradation]] |
| - | + | ||
| - | + | ||
[[Category: local structure]] | [[Category: local structure]] | ||
[[Category: lpl]] | [[Category: lpl]] | ||
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[[Category: structure]] | [[Category: structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:41:36 2008'' |
Revision as of 19:41, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLOBAL STRUCTURE AND DYNAMICS OF HUMAN APOLIPOPROTEIN CII IN COMPLEX WITH MICELLES: EVIDENCE FOR INCREASED MOBILITY OF THE HELIX INVOLVVED IN THE ACTIVATION OF LIPOPROTEIN LIPASE.
Overview
Apolipoprotein CII (apoCII), a surface constituent of plasma lipoproteins, is the activator for lipoprotein lipase (LPL) and is therefore central for lipid transport in blood. The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported. In addition to the structure determination, (15)N-relaxation measurements have been performed at two magnetic fields to characterize the dynamics of the backbone of apoCII in the complex. The relaxation data also provided global structural constraints, viz. the orientation of helices in the complex. In addition, global constraints were derived from the fact that apoCII helices are attached to the surface of the SDS micelle and that the hydrophobic moments of each helix faces the interior of the micelle. These three categories of global constraints, together with the local classical NMR constraints, were sufficient to define the 3D structure of the apoCII-SDS micelle complex. To our knowledge, this presents the first example in which the global structure of a protein-SDS micelle complex has been determined. The C-terminal helix of apoCII is known to be responsible for the activation of LPL. This helix is distinguished from the other helices by a higher degree of internal motion on the nanosecond time scale as shown by the relaxation data. The overall structure and the internal dynamics, combined with previous mutation data, give important clues toward a possible mechanism for the activation of LPL by apoCII.
About this Structure
1O8T is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase., Zdunek J, Martinez GV, Schleucher J, Lycksell PO, Yin Y, Nilsson S, Shen Y, Olivecrona G, Wijmenga S, Biochemistry. 2003 Feb 25;42(7):1872-89. PMID:12590574
Page seeded by OCA on Sun Mar 30 22:41:36 2008
Categories: Homo sapiens | Single protein | Lycksell, P O. | Martinez, G V. | Nilsson, S. | Olivecrona, G. | Schleucher, J. | Shen, Y. | Wijmenga, S. | Yin, Y. | Zdunek, J. | Activation mechanism | Apocii | Chylomicron | Domain motion | Dynamic | Global structure | Helix ,lipid transport,lipid degradation | Local structure | Lpl | Micelle | Sd | Structure
