1j2e

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[[Image:1j2e.jpg|left|200px]]<br /><applet load="1j2e" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j2e.jpg|left|200px]]
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caption="1j2e, resolution 2.6&Aring;" />
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'''Crystal structure of Human Dipeptidyl peptidase IV'''<br />
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{{Structure
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|PDB= 1j2e |SIZE=350|CAPTION= <scene name='initialview01'>1j2e</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal structure of Human Dipeptidyl peptidase IV'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1J2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2E OCA].
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1J2E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2E OCA].
==Reference==
==Reference==
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The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold., Hiramatsu H, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Yamamoto A, Shimizu R, Biochem Biophys Res Commun. 2003 Mar 21;302(4):849-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12646248 12646248]
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The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold., Hiramatsu H, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Yamamoto A, Shimizu R, Biochem Biophys Res Commun. 2003 Mar 21;302(4):849-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12646248 12646248]
[[Category: Dipeptidyl-peptidase IV]]
[[Category: Dipeptidyl-peptidase IV]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:58:00 2008''

Revision as of 09:58, 20 March 2008

Image:1j2e.jpg


PDB ID 1j2e

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands:
Activity: Dipeptidyl-peptidase IV, with EC number 3.4.14.5
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Human Dipeptidyl peptidase IV


Overview

Dipeptidyl peptidase IV (DPPIV) is a serine protease, a member of the prolyl oligopeptidase (POP) family, and has been implicated in several diseases. Therefore, the development of DPPIV selective inhibitors, which are able to control the biological function of DPPIV, is important. We determined the crystal structure of human DPPIV at 2.6A resolution. The molecule consists of a unique eight-bladed beta-propeller domain in the N-terminal region and a serine protease domain in the C-terminal region. Also, the large "cave" structure, which is thought to control the access of the substrate, is found on the side of the beta-propeller fold. Comparison of the overall amino acid sequence between human DPPIV and POP shows low homology (12.9%). In this paper, we report the structure of human DPPIV, especially focusing on a unique eight-bladed beta-propeller domain. We also discuss the way for the access of the substrate to this domain.

About this Structure

1J2E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold., Hiramatsu H, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Yamamoto A, Shimizu R, Biochem Biophys Res Commun. 2003 Mar 21;302(4):849-54. PMID:12646248

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