1len

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[[Image:1len.gif|left|200px]]
 
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{{Structure
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==REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION==
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|PDB= 1len |SIZE=350|CAPTION= <scene name='initialview01'>1len</scene>, resolution 1.8&Aring;
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<StructureSection load='1len' size='340' side='right'caption='[[1len]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1len]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LEN FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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|DOMAIN=
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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=1len FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1len OCA], [https://pdbe.org/1len PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1len RCSB], [https://www.ebi.ac.uk/pdbsum/1len PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1len ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1len FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1len OCA], [http://www.ebi.ac.uk/pdbsum/1len PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1len RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LEC_LENCU LEC_LENCU] D-mannose specific lectin (By similarity).
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== Evolutionary Conservation ==
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'''REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/le/1len_consurf.spt"</scriptWhenChecked>
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The structures of two crystal forms of lentil lectin are determined and refined at high resolution. Orthorhombic lentil lectin is refined at 1.80 A resolution to an R-factor of 0.184 and monoclinic lentil lectin at 1.75 A resolution to an R-factor of 0.175. These two structures are compared to each other and to the other available legume lectin structures. The monosaccharide binding pocket of each lectin monomer contains a tightly bound phosphate ion. This phosphate makes hydrogen bonding contacts with Asp-81 beta, Gly-99 beta, and Asn-125 beta, three residues that are highly conserved in most of the known legume lectin sequences and essential for monosaccharide recognition in all legume lectin crystal structures described thus far. A detailed analysis of the composition and properties of the hydrophobic contact network and hydrophobic nuclei in lentil lectin is presented. Contact map calculations reveal that dense clusters of nonpolar as well as polar side chains play a major role in secondary structure packing. This is illustrated by a large cluster of 24 mainly hydrophobic amino acids that is responsible for the majority of packing interactions between the two beta-sheets. Another series of four smaller and less hydrophobic clusters is found to mediate the packing of a number of loop structures upon the front sheet. A very dense, but not very conserved cluster is found to stabilize the transition metal binding site. The highly conserved and invariant nonpolar residues are distributed asymmetrically over the protein.
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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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==About this Structure==
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</jmolCheckbox>
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1LEN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lens_culinaris Lens culinaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEN OCA].
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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=1len ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution., Loris R, Van Overberge D, Dao-Thi MH, Poortmans F, Maene N, Wyns L, Proteins. 1994 Dec;20(4):330-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7731952 7731952]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Lens culinaris]]
[[Category: Lens culinaris]]
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[[Category: Protein complex]]
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[[Category: Loris R]]
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[[Category: Loris, R.]]
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[[Category: Van Overberge D]]
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[[Category: Overberge, D Van.]]
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[[Category: Wyns L]]
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[[Category: Wyns, L.]]
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[[Category: lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:54 2008''
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Current revision

REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION

PDB ID 1len

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