1m7l

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7l OCA], [http://www.ebi.ac.uk/pdbsum/1m7l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m7l RCSB]</span>
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'''Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D'''
'''Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D'''
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[[Category: Nilges, M.]]
[[Category: Nilges, M.]]
[[Category: Reid, K B.M.]]
[[Category: Reid, K B.M.]]
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[[Category: ambiguous distance restraint]]
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[[Category: Ambiguous distance restraint]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: lung surfactant protein]]
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[[Category: Lung surfactant protein]]
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[[Category: nmr-spectroscopy]]
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[[Category: Nmr-spectroscopy]]
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[[Category: trimer]]
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[[Category: Trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:44:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:27 2008''
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Revision as of 21:44, 2 May 2008

Template:STRUCTURE 1m7l

Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D


Overview

Surfactant protein D (SP-D) is one of four known protein components of the pulmonary surfactant lining the lung alveoli. It is involved in immune and allergic responses. SP-D occurs as a tetramer of trimers. Trimerization is thought to be initiated by a coiled coil domain. We have determined the solution structure of a 64-residue peptide encompassing the coiled coil domain of human SP-D. As predicted, the domain forms a triple-helical parallel coiled coil. As with all symmetric oligomers, the structure calculation was complicated by the symmetry degeneracy in the NMR spectra. We used the symmetry-ADR (ambiguous distance restraint) structure calculation method to solve the structure. The results demonstrate that the leucine zipper region of SP-D is an autonomously folded domain. The structure is very similar to the independently determined X-ray crystal structure, differing mainly at a single residue, Tyr248. This residue is completely symmetric in the solution structure, and markedly asymmetric in the crystalline phase. This difference may be functionally important, as it affects the orientation of the antigenic surface presented by SP-D.

About this Structure

1M7L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the coiled-coil trimerization domain from lung surfactant protein D., Kovacs H, O'Ddonoghue SI, Hoppe HJ, Comfort D, Reid KB, Campbell D, Nilges M, J Biomol NMR. 2002 Oct;24(2):89-102. PMID:12495025 Page seeded by OCA on Sat May 3 00:44:01 2008

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