7v4s: Difference between revisions
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==Horcolin complex with methyl-alpha-mannose== | ==Horcolin complex with methyl-alpha-mannose== | ||
<StructureSection load='7v4s' size='340' side='right'caption='[[7v4s]]' scene=''> | <StructureSection load='7v4s' size='340' side='right'caption='[[7v4s]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V4S FirstGlance]. <br> | <table><tr><td colspan='2'>[[7v4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V4S FirstGlance]. <br> | ||
</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=7v4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4s OCA], [https://pdbe.org/7v4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4s RCSB], [https://www.ebi.ac.uk/pdbsum/7v4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4s ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</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=7v4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v4s OCA], [https://pdbe.org/7v4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v4s RCSB], [https://www.ebi.ac.uk/pdbsum/7v4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v4s ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/LECH_HORVU LECH_HORVU]] Mannose-specific lectin. Has a weak agglutinating activity against rabbit erythrocytes (By similarity).[UniProtKB:P82953] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lectins are sugar-binding proteins that have shown considerable promise as antiviral agents because of their ability to interact with envelope glycoproteins present on the surface of viruses such as HIV-1. However, their therapeutic potential has been compromised by their mitogenicity that stimulates uncontrolled division of T-lymphocytes. Horcolin, a member of the jacalin family of lectins, tightly binds the HIV-1 envelope glycoprotein gp120 and neutralizes HIV-1 particles but is nonmitogenic. In this report, we combine X-ray crystallography and NMR spectroscopy to obtain atomic-resolution insights into the structure of horcolin and the molecular basis for its carbohydrate recognition. Each protomer of the horcolin dimer adopts a canonical beta-prism I fold with three Greek key motifs and carries two carbohydrate-binding sites. The carbohydrate molecule binds in a negatively charged pocket and is stabilized by backbone and side chain hydrogen bonds to conserved residues in the ligand-binding loop. NMR titrations reveal a two-site binding mode and equilibrium dissociation constants for the two binding sites determined from two-dimensional (2D) lineshape modeling are 4-fold different. Single-binding-site variants of horcolin confirm the dichotomy in binding sites and suggest that there is allosteric communication between the two sites. An analysis of the horcolin structure shows a network of hydrogen bonds linking the two carbohydrate-binding sites directly and through a secondary binding site, and this coupling between the two sites is expected to assume importance in the interaction of horcolin with high-mannose glycans found on viral envelope glycoproteins. | |||
Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin.,Narayanan V, Bobbili KB, Sivaji N, Jayaprakash NG, Suguna K, Surolia A, Sekhar A Biochemistry. 2022 Feb 28. doi: 10.1021/acs.biochem.1c00778. PMID:35225598<ref>PMID:35225598</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7v4s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bobbili | [[Category: Bobbili, K B]] | ||
[[Category: Jayaprakash | [[Category: Jayaprakash, N G]] | ||
[[Category: Narayanan V]] | [[Category: Narayanan, V]] | ||
[[Category: Sekhar A]] | [[Category: Sekhar, A]] | ||
[[Category: Sivaji N]] | [[Category: Sivaji, N]] | ||
[[Category: Suguna K]] | [[Category: Suguna, K]] | ||
[[Category: Surolia A]] | [[Category: Surolia, A]] | ||
[[Category: Horcolin]] | |||
[[Category: Mannose-binding lectin]] | |||
[[Category: Sugar binding protein]] | |||
