This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1r54

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 16:06, 12 October 2017

Crystal structure of the catalytic domain of human ADAM33

Structural highlights

1r54 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1r55
Gene:	ADAM33 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ADA33_HUMAN] Genetic variations in ADAM33 are associated with susceptibility to asthma (ASTHMA) [MIM:600807]. The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with weezing due to spasmodic contraction of the bronchi.^[1] ^[2] ^[3]

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 PubMed

Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme.

Crystal structure of the catalytic domain of human ADAM33.,Orth P, Reichert P, Wang W, Prosise WW, Yarosh-Tomaine T, Hammond G, Ingram RN, Xiao L, Mirza UA, Zou J, Strickland C, Taremi SS, Le HV, Madison V J Mol Biol. 2004 Jan 2;335(1):129-37. PMID:14659745^[4]

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

References

↑ Van Eerdewegh P, Little RD, Dupuis J, Del Mastro RG, Falls K, Simon J, Torrey D, Pandit S, McKenny J, Braunschweiger K, Walsh A, Liu Z, Hayward B, Folz C, Manning SP, Bawa A, Saracino L, Thackston M, Benchekroun Y, Capparell N, Wang M, Adair R, Feng Y, Dubois J, FitzGerald MG, Huang H, Gibson R, Allen KM, Pedan A, Danzig MR, Umland SP, Egan RW, Cuss FM, Rorke S, Clough JB, Holloway JW, Holgate ST, Keith TP. Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness. Nature. 2002 Jul 25;418(6896):426-30. Epub 2002 Jul 10. PMID:12110844 doi:10.1038/nature00878
↑ Kedda MA, Duffy DL, Bradley B, O'Hehir RE, Thompson PJ. ADAM33 haplotypes are associated with asthma in a large Australian population. Eur J Hum Genet. 2006 Sep;14(9):1027-36. Epub 2006 Jun 14. PMID:16773130 doi:10.1038/sj.ejhg.5201662
↑ Blakey JD, Sayers I, Ring SM, Strachan DP, Hall IP. Positionally cloned asthma susceptibility gene polymorphisms and disease risk in the British 1958 Birth Cohort. Thorax. 2009 May;64(5):381-7. doi: 10.1136/thx.2008.102053. Epub 2009 Feb 22. PMID:19237393 doi:10.1136/thx.2008.102053
↑ Orth P, Reichert P, Wang W, Prosise WW, Yarosh-Tomaine T, Hammond G, Ingram RN, Xiao L, Mirza UA, Zou J, Strickland C, Taremi SS, Le HV, Madison V. Crystal structure of the catalytic domain of human ADAM33. J Mol Biol. 2004 Jan 2;335(1):129-37. PMID:14659745

1 Structural highlights
2 Disease
3 Evolutionary Conservation
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/1r54"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the catalytic domain of human ADAM33==
 <StructureSection load='1r54' size='340' side='right' caption='[[1r54]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1r54]] is a 1 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=1R54 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R54 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r55|1r55]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADAM33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1r54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r54 OCA], [http://pdbe.org/1r54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r54 RCSB], [http://www.ebi.ac.uk/pdbsum/1r54 PDBsum]</span></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=1r54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r54 OCA], [http://pdbe.org/1r54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r54 RCSB], [http://www.ebi.ac.uk/pdbsum/1r54 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r54 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1r54" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[A Disintegrin And Metalloproteinase|A Disintegrin And Metalloproteinase]]
 == References ==
 <references/>

1r54

From Proteopedia

Revision as of 16:06, 12 October 2017

Crystal structure of the catalytic domain of human ADAM33

Structural highlights

Disease

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox