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1w1i

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[[Image:1w1i.gif|left|200px]]<br /><applet load="1w1i" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1w1i, resolution 3.03&Aring;" />
 
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'''CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR CD26) IN COMPLEX WITH ADENOSINE DEAMINASE'''<br />
 
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==Overview==
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==Crystal structure of dipeptidyl peptidase IV (DPPIV or CD26) in complex with adenosine deaminase==
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Dipeptidyl-peptidase IV (DPPIV or CD26) is a homodimeric type II membrane, glycoprotein in which the two monomers are subdivided into a, beta-propeller domain and an alpha/beta-hydrolase domain. As dipeptidase, DPPIV modulates the activity of various biologically important peptides, and, in addition, DPPIV acts as a receptor for adenosine deaminase (ADA), thereby mediating co-stimulatory signals in T-lymphocytes. The 3.0-A, resolution crystal structure of the complex formed between human DPPIV and, bovine ADA presented here shows that each beta-propeller domain of the, DPPIV dimer binds one ADA. At the binding interface, two hydrophobic loops, protruding from the beta-propeller domain of DPPIV interact with two, hydrophilic and heavily charged alpha-helices of ADA, giving rise to the, highest percentage of charged residues involved in a protein-protein, contact reported thus far. Additionally, four glycosides linked to Asn229, of DPPIV bind to ADA. In the crystal structure of porcine DPPIV, the, observed tetramer formation was suggested to mediate epithelial and, lymphocyte cell-cell adhesion. ADA binding to DPPIV could regulate this, adhesion, as it would abolish tetramerization.
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<StructureSection load='1w1i' size='340' side='right'caption='[[1w1i]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1w1i]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W1I FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.03&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w1i OCA], [https://pdbe.org/1w1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w1i RCSB], [https://www.ebi.ac.uk/pdbsum/1w1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w1i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADA_BOVIN ADA_BOVIN] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w1/1w1i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1w1i ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dipeptidyl-peptidase IV (DPPIV or CD26) is a homodimeric type II membrane glycoprotein in which the two monomers are subdivided into a beta-propeller domain and an alpha/beta-hydrolase domain. As dipeptidase, DPPIV modulates the activity of various biologically important peptides and, in addition, DPPIV acts as a receptor for adenosine deaminase (ADA), thereby mediating co-stimulatory signals in T-lymphocytes. The 3.0-A resolution crystal structure of the complex formed between human DPPIV and bovine ADA presented here shows that each beta-propeller domain of the DPPIV dimer binds one ADA. At the binding interface, two hydrophobic loops protruding from the beta-propeller domain of DPPIV interact with two hydrophilic and heavily charged alpha-helices of ADA, giving rise to the highest percentage of charged residues involved in a protein-protein contact reported thus far. Additionally, four glycosides linked to Asn229 of DPPIV bind to ADA. In the crystal structure of porcine DPPIV, the observed tetramer formation was suggested to mediate epithelial and lymphocyte cell-cell adhesion. ADA binding to DPPIV could regulate this adhesion, as it would abolish tetramerization.
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==About this Structure==
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Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface.,Weihofen WA, Liu J, Reutter W, Saenger W, Fan H J Biol Chem. 2004 Oct 8;279(41):43330-5. Epub 2004 Jun 22. PMID:15213224<ref>PMID:15213224</ref>
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1W1I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, NDG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] Known structural/functional Site: <scene name='pdbsite=AC1:Zn Binding Site For Chain H'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W1I OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface., Weihofen WA, Liu J, Reutter W, Saenger W, Fan H, J Biol Chem. 2004 Oct 8;279(41):43330-5. Epub 2004 Jun 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15213224 15213224]
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</div>
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<div class="pdbe-citations 1w1i" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
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*[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Dipeptidyl-peptidase IV]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Fan, H.]]
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[[Category: Fan H]]
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[[Category: Liu, J.]]
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[[Category: Liu J]]
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[[Category: Reutter, W.]]
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[[Category: Reutter W]]
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[[Category: Saenger, W.]]
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[[Category: Saenger W]]
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[[Category: Weihofen, W.A.]]
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[[Category: Weihofen WA]]
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[[Category: NAG]]
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[[Category: NDG]]
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[[Category: ZN]]
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[[Category: ada]]
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[[Category: adenosine deaminase]]
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[[Category: alpha/beta-hydrolase fold]]
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[[Category: aminopeptidase]]
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[[Category: beta-propeller fold]]
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[[Category: cd26]]
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[[Category: dipetidyl peptidase iv]]
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[[Category: dppiv]]
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[[Category: protein-protein complex]]
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[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:26:11 2007''
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Current revision

Crystal structure of dipeptidyl peptidase IV (DPPIV or CD26) in complex with adenosine deaminase

PDB ID 1w1i

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