1m7l

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[[Image:1m7l.jpg|left|200px]]
 
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==Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D==
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The line below this paragraph, containing "STRUCTURE_1m7l", creates the "Structure Box" on the page.
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<StructureSection load='1m7l' size='340' side='right'caption='[[1m7l]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m7l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7l OCA], [https://pdbe.org/1m7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7l RCSB], [https://www.ebi.ac.uk/pdbsum/1m7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7l ProSAT]</span></td></tr>
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{{STRUCTURE_1m7l| PDB=1m7l | SCENE= }}
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</table>
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== Function ==
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'''Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D'''
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[https://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/1m7l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m7l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==About this Structure==
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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<ref>PMID:12495025</ref>
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1M7L is a [[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=1M7L OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12495025 12495025]
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</div>
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<div class="pdbe-citations 1m7l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Campbell, I D.]]
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[[Category: Campbell ID]]
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[[Category: Comfort, D.]]
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[[Category: Comfort D]]
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[[Category: Donoghue, S I.O.]]
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[[Category: Hoppe H-J]]
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[[Category: Hoppe, H J.]]
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[[Category: Kovacs H]]
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[[Category: Kovacs, H.]]
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[[Category: Nilges M]]
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[[Category: Nilges, M.]]
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[[Category: O'Donoghue SI]]
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[[Category: Reid, K B.M.]]
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[[Category: Reid KBM]]
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[[Category: Ambiguous distance restraint]]
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[[Category: Coiled coil]]
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[[Category: Lung surfactant protein]]
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[[Category: Nmr-spectroscopy]]
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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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Current revision

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

PDB ID 1m7l

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