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< | ==Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG, bound to sucrose== | ||
<StructureSection load='3hp8' size='340' side='right'caption='[[3hp8]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hp8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] and [https://en.wikipedia.org/wiki/Tuber_borchii Tuber borchii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HP8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=3hp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hp8 OCA], [https://pdbe.org/3hp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hp8 RCSB], [https://www.ebi.ac.uk/pdbsum/3hp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hp8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CVNH_NEUCR CVNH_NEUCR] Mannose-binding lectin.<ref>PMID:18400178</ref> [https://www.uniprot.org/uniprot/CVNH_TUBBO CVNH_TUBBO] Mannose-binding lectin.<ref>PMID:18400178</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/3hp8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3hp8 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The NMR and X-ray structures of a designed chimeric cyanovirin-N homolog (CVNH) protein were determined. The individual halves of the structure are similar to their counterparts in the parent proteins, with domains A and B resembling the structures of TbCVNH and NcCVNH, respectively. No significant differences between the solution and crystal conformations were observed, although details in loop conformations and distinct crystal packing-induced features are present. Carbohydrate binding studies by NMR revealed affinity and specificity for Glc alpha(1-2)Frc and Man alpha(1-2)Man, and the parental half that is devoid of any sucrose affinity in NcCVNH was transformed into a genuine sucrose binding site in the context of the chimera. The atomic details of sugar recognition are seen in the crystal structure of the protein with two bound Glc alpha(1-2)Frc molecules. Both sugars exhibit different conformations around the glycosidic bond and engage in unique hydrogen bonding networks in the two sites. Although the protein is able to bind two Man alpha(1-2)Man molecules, a property associated with HIV-inactivation, no anti-HIV activity was observed for the hybrid protein. These results provide the structural basis for sugar recognition in the CVNH family and aid in deciphering the relationship between sugar binding and anti-HIV activity. | |||
A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding.,Koharudin LM, Furey W, Gronenborn AM Proteins. 2009 Dec;77(4):904-15. PMID:19639634<ref>PMID:19639634</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3hp8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
= | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neurospora crassa]] | |||
[[Category: | [[Category: Tuber borchii]] | ||
[[Category: | [[Category: Furey W]] | ||
[[Category: | [[Category: Gronenborn AM]] | ||
[[Category: | [[Category: Koharudin LMI]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 10:25, 6 September 2023
Crystal structure of a designed Cyanovirin-N homolog lectin; LKAMG, bound to sucroseCrystal structure of a designed Cyanovirin-N homolog lectin; LKAMG, bound to sucrose
Structural highlights
FunctionCVNH_NEUCR Mannose-binding lectin.[1] CVNH_TUBBO Mannose-binding lectin.[2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe NMR and X-ray structures of a designed chimeric cyanovirin-N homolog (CVNH) protein were determined. The individual halves of the structure are similar to their counterparts in the parent proteins, with domains A and B resembling the structures of TbCVNH and NcCVNH, respectively. No significant differences between the solution and crystal conformations were observed, although details in loop conformations and distinct crystal packing-induced features are present. Carbohydrate binding studies by NMR revealed affinity and specificity for Glc alpha(1-2)Frc and Man alpha(1-2)Man, and the parental half that is devoid of any sucrose affinity in NcCVNH was transformed into a genuine sucrose binding site in the context of the chimera. The atomic details of sugar recognition are seen in the crystal structure of the protein with two bound Glc alpha(1-2)Frc molecules. Both sugars exhibit different conformations around the glycosidic bond and engage in unique hydrogen bonding networks in the two sites. Although the protein is able to bind two Man alpha(1-2)Man molecules, a property associated with HIV-inactivation, no anti-HIV activity was observed for the hybrid protein. These results provide the structural basis for sugar recognition in the CVNH family and aid in deciphering the relationship between sugar binding and anti-HIV activity. A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding.,Koharudin LM, Furey W, Gronenborn AM Proteins. 2009 Dec;77(4):904-15. PMID:19639634[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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