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1efq

From Proteopedia

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{{Seed}}
 
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[[Image:1efq.png|left|200px]]
 
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==Q38D mutant of LEN==
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The line below this paragraph, containing "STRUCTURE_1efq", creates the "Structure Box" on the page.
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<StructureSection load='1efq' size='340' side='right'caption='[[1efq]], [[Resolution|resolution]] 1.60&Aring;' 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'>[[1efq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFQ 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">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1efq| PDB=1efq | SCENE= }}
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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=1efq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efq OCA], [https://pdbe.org/1efq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efq RCSB], [https://www.ebi.ac.uk/pdbsum/1efq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efq ProSAT]</span></td></tr>
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</table>
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===Q38D mutant of LEN===
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== Function ==
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[https://www.uniprot.org/uniprot/KV401_HUMAN KV401_HUMAN] V segment of the variable domain of immunoglobulins light chain that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170).<ref>PMID:17576170</ref> <ref>PMID:20176268</ref> <ref>PMID:22158414</ref> <ref>PMID:24600447</ref>
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== Evolutionary Conservation ==
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<!--
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[[Image:Consurf_key_small.gif|200px|right]]
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The line below this paragraph, {{ABSTRACT_PUBMED_12070321}}, adds the Publication Abstract to the page
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Check<jmol>
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(as it appears on PubMed at http://www.pubmed.gov), where 12070321 is the PubMed ID number.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/1efq_consurf.spt"</scriptWhenChecked>
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{{ABSTRACT_PUBMED_12070321}}
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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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1EFQ 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=1EFQ 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=1efq ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Factors contributing to decreased protein stability when aspartic acid residues are in beta-sheet regions., Pokkuluri PR, Gu M, Cai X, Raffen R, Stevens FJ, Schiffer M, Protein Sci. 2002 Jul;11(7):1687-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12070321 12070321]
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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: Cai, X.]]
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[[Category: Cai X]]
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[[Category: Gu, M.]]
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[[Category: Gu M]]
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[[Category: Pokkuluri, P R.]]
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[[Category: Pokkuluri PR]]
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[[Category: Schiffer, M.]]
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[[Category: Schiffer M]]
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[[Category: Stevens, F J.]]
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[[Category: Stevens FJ]]
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[[Category: Aspartic acid in beta-sheet]]
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[[Category: Human kappa-4 immunoglobulin light chain]]
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[[Category: Monomer]]
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[[Category: Mutant]]
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[[Category: Protein stability]]
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[[Category: Uranyl ion in crystal contact]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:37:26 2008''
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Current revision

Q38D mutant of LEN

PDB ID 1efq

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