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5h7n

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Current revision

Crystal structure of human NLRP12-PYD with a MBP tag

Structural highlights

5h7n is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.849Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

NAL12_HUMAN NLRP12-associated hereditary periodic fever syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.NAL12_HUMAN May mediate activation of CASP1 via ASC and promote activation of NF-kappa-B via IKK.

Publication Abstract from PubMed

Crystallization chaperones have been used to facilitate the crystallization of challenging proteins. Even though the maltose-binding protein (MBP) is one of the most commonly used crystallization chaperones, the design of optimal expression constructs for crystallization of MBP fusion proteins remains a challenge. To increase the success rate of MBP-facilitated crystallization, a series of expression vectors have been designed with either a short flexible linker or a set of rigid helical linkers. Seven death domain superfamily members were tested for crystallization with this set of vectors, six of which had never been crystallized before. All of the seven targets were crystallized, and their structures were determined using at least one of the vectors. Our successful crystallization of all of the targets demonstrates the validity of our approach and expands the arsenal of the crystallization chaperone toolkit, which may be applicable to crystallization of other difficult protein targets, as well as to other crystallization chaperones.

Design of an expression system to enhance MBP-mediated crystallization.,Jin T, Chuenchor W, Jiang J, Cheng J, Li Y, Fang K, Huang M, Smith P, Xiao TS Sci Rep. 2017 Jan 23;7:40991. doi: 10.1038/srep40991. PMID:28112203^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jin T, Chuenchor W, Jiang J, Cheng J, Li Y, Fang K, Huang M, Smith P, Xiao TS. Design of an expression system to enhance MBP-mediated crystallization. Sci Rep. 2017 Jan 23;7:40991. doi: 10.1038/srep40991. PMID:28112203 doi:http://dx.doi.org/10.1038/srep40991

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5h7n"

Categories: Homo sapiens | Large Structures | Jin TC | Xiao TS

@@ Line 3: / Line 3: @@
 <StructureSection load='5h7n' size='340' side='right'caption='[[5h7n]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h7n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H7N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H7N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5h7n]] 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=5H7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H7N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MTT:MALTOTETRAOSE'>MTT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.849&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h7q|5h7q]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7n OCA], [http://pdbe.org/5h7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h7n RCSB], [http://www.ebi.ac.uk/pdbsum/5h7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7n ProSAT]</span></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=5h7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7n OCA], [https://pdbe.org/5h7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h7n RCSB], [https://www.ebi.ac.uk/pdbsum/5h7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7n ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/NAL12_HUMAN NAL12_HUMAN] NLRP12-associated hereditary periodic fever syndrome. The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/NAL12_HUMAN NAL12_HUMAN] May mediate activation of CASP1 via ASC and promote activation of NF-kappa-B via IKK.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Jin, T C]]
+[[Category: Jin TC]]
-[[Category: Xiao, T S]]
+[[Category: Xiao TS]]
-[[Category: Crystallization tag]]
-[[Category: Death fold]]
-[[Category: Maltose binding protein]]
-[[Category: Sugar binding protein]]

5h7n

From Proteopedia

Current revision

Crystal structure of human NLRP12-PYD with a MBP tag

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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