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==Crystal structure of ligand-free VRC03 antigen-binding fragment.==
==Crystal structure of ligand-free VRC03 antigen-binding fragment.==
<StructureSection load='5jxa' size='340' side='right' caption='[[5jxa]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5jxa' size='340' side='right'caption='[[5jxa]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5jxa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JXA FirstGlance]. <br>
<table><tr><td colspan='2'>[[5jxa]] is a 2 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=5JXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JXA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxa OCA], [http://pdbe.org/5jxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jxa RCSB], [http://www.ebi.ac.uk/pdbsum/5jxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxa ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxa OCA], [https://pdbe.org/5jxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jxa RCSB], [https://www.ebi.ac.uk/pdbsum/5jxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxa ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibody somatic hypermutation (SHM) and affinity maturation enhance antigen recognition by modifying antibody paratope structure to improve its complementarity with the target epitope. SHM-induced changes in paratope dynamics may also contribute to antibody maturation, but direct evidence of this is limited. Here, we examine two classes of HIV-1 broadly neutralizing antibodies (bNAbs) for SHM-induced changes in structure and dynamics, and delineate the effects of these changes on interactions with the HIV-1 envelope glycoprotein (Env). In combination with new and existing structures of unmutated and affinity matured antibody Fab fragments, we used hydrogen/deuterium exchange with mass spectrometry to directly measure Fab structural dynamics. Changes in antibody structure and dynamics were positioned to improve complementarity with Env, with changes in dynamics primarily observed at the paratope peripheries. We conclude that SHM optimizes paratope complementarity to conserved HIV-1 epitopes and restricts the mobility of paratope-peripheral residues to minimize clashes with variable features on HIV-1 Env.
Somatic Hypermutation-Induced Changes in the Structure and Dynamics of HIV-1 Broadly Neutralizing Antibodies.,Davenport TM, Gorman J, Joyce MG, Zhou T, Soto C, Guttman M, Moquin S, Yang Y, Zhang B, Doria-Rose NA, Hu SL, Mascola JR, Kwong PD, Lee KK Structure. 2016 Jul 20. pii: S0969-2126(16)30139-3. doi:, 10.1016/j.str.2016.06.012. PMID:27477385<ref>PMID:27477385</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jxa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Joyce, M G]]
[[Category: Homo sapiens]]
[[Category: Kwong, P D]]
[[Category: Large Structures]]
[[Category: Mascola, J R]]
[[Category: Joyce MG]]
[[Category: Moquin, S]]
[[Category: Kwong PD]]
[[Category: Zhou, T]]
[[Category: Mascola JR]]
[[Category: Antibody development]]
[[Category: Moquin S]]
[[Category: Cd4 binding site]]
[[Category: Zhou T]]
[[Category: Hiv-1]]
[[Category: Immune system]]
[[Category: Neutralizing]]
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