1hp7
From Proteopedia
(New page: 200px<br /> <applet load="1hp7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hp7, resolution 2.1Å" /> '''A 2.1 ANGSTROM STRUC...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hp7. | + | [[Image:1hp7.jpg|left|200px]]<br /><applet load="1hp7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hp7" size=" | + | |
caption="1hp7, resolution 2.1Å" /> | caption="1hp7, resolution 2.1Å" /> | ||
'''A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS'''<br /> | '''A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HP7 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 ZN and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HP7 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=ZN:'>ZN</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HP7 OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 25: | ||
[[Category: uncleaved alpha-1-antitrypsin serpin]] | [[Category: uncleaved alpha-1-antitrypsin serpin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:35 2008'' |
Revision as of 13:57, 15 February 2008
|
A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS
Contents |
Overview
Serpin (serine protease inhibitor) proteins are involved in diverse, physiological processes including inflammation, coagulation, matrix, remodeling, and cell differentiation. Deficiency of normal serpin, functions leads to various hereditary diseases. Besides their clinical, importance, serpin proteins draw much attention due to the large, conformational changes that occur upon interaction with proteases. We, present here the crystal structure of an uncleaved alpha(1)-antitrypsin, determined by the multiple isomorphous replacement method and refined to, 2.1 A resolution. The structure, which is the first active serpin, structure based on experimental phases, reveals novel conformations in the, flexible loops, including the proximal hinge region of the reactive center, loop and the surface cavity region in the central beta-sheet, sheet A. The, determined loop conformation explains the results of recent mutagenesis, studies and provides detailed insights into the protease inhibition, mechanism. The high-resolution structure of active alpha(1)-antitrypsin, also provides evidence for the existence of localized van-der-Waals strain, in the central hydrophobic core.
Disease
Known diseases associated with this structure: Emphysema OMIM:[107400], Emphysema-cirrhosis OMIM:[107400], Hemorrhagic diathesis due to antithrombin Pittsburgh OMIM:[107400], Pulmonary disease, chronic obstructive, susceptibility to OMIM:[107400]
About this Structure
1HP7 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops., Kim S, Woo J, Seo EJ, Yu M, Ryu S, J Mol Biol. 2001 Feb 9;306(1):109-19. PMID:11178897
Page seeded by OCA on Fri Feb 15 15:57:35 2008
