2ptl

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[[Image:2ptl.jpg|left|200px]]
 
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{{Structure
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==THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN-BINDING DOMAIN OF PROTEIN L. COMPARISON WITH THE IGG-BINDING DOMAINS OF PROTEIN G==
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|PDB= 2ptl |SIZE=350|CAPTION= <scene name='initialview01'>2ptl</scene>
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<StructureSection load='2ptl' size='340' side='right'caption='[[2ptl]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2ptl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna_ATCC_29328 Finegoldia magna ATCC 29328]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PTL 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">Solution NMR</td></tr>
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|GENE=
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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=2ptl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ptl OCA], [https://pdbe.org/2ptl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ptl RCSB], [https://www.ebi.ac.uk/pdbsum/2ptl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ptl ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN-BINDING DOMAIN OF PROTEIN L. COMPARISON WITH THE IGG-BINDING DOMAINS OF PROTEIN G'''
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[https://www.uniprot.org/uniprot/Q53291_FINMA Q53291_FINMA]
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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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Protein L is a multidomain protein expressed at the surface of some strains of the anaerobic bacterial species Peptostreptococcus magnus. It has affinity for immunoglobulin (Ig) through interaction with framework structures in the variable Ig light chain domain. The Ig-binding activity is located to five homologous repeats called B1-B5 in the N-terminal part of the protein. We have determined the three-dimensional solution structure of the 76 amino acid residue long B1 domain using NMR spectroscopy and distance geometry-restrained simulated annealing. The domain is composed of a 15 amino acid residue long disordered N-terminus followed by a folded portion comprising an alpha-helix packed against a four-stranded beta-sheet. These secondary structural elements are well determined with a backbone atomic root mean square deviation from their mean of 0.54 A. The B domains of protein L show very limited sequence homology to the domains of streptococcal protein G interacting with the heavy chains of IgG. However, despite this fact, and their different binding properties, the fold of the B1 domain was found to be similar to the fold of the IgG-binding protein G domains [Wikstrom, M., Sjobring, U., Kastern, W., Bjorck, L., Drakenberg, T., &amp; Forsen, S. (1993) Biochemistry 32, 3381-3386]. In the present study, the solution structure of the B1 domain enabled a more detailed comparison which can explain the different Ig-binding specificities of these two bacterial surface proteins. Among the differences observed, the alpha-helix orientation is the most striking.(ABSTRACT TRUNCATED AT 250 WORDS)
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/2ptl_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2PTL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTL OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=2ptl ConSurf].
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Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G., Wikstrom M, Drakenberg T, Forsen S, Sjobring U, Bjorck L, Biochemistry. 1994 Nov 29;33(47):14011-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7947810 7947810]
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<div style="clear:both"></div>
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[[Category: Finegoldia magna]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Bjoerck, L.]]
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[[Category: Finegoldia magna ATCC 29328]]
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[[Category: Drakenberg, T.]]
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[[Category: Large Structures]]
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[[Category: Forsen, S.]]
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[[Category: Bjoerck L]]
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[[Category: Sjoebring, U.]]
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[[Category: Drakenberg T]]
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[[Category: Wikstroem, M.]]
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[[Category: Forsen S]]
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[[Category: binding protein(immunoglobulin l chain)]]
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[[Category: Sjoebring U]]
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[[Category: Wikstroem M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:17:12 2008''
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Current revision

THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN-BINDING DOMAIN OF PROTEIN L. COMPARISON WITH THE IGG-BINDING DOMAINS OF PROTEIN G

PDB ID 2ptl

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