|
|
| Line 1: |
Line 1: |
| [[Image:1kn6.gif|left|200px]] | | {{Seed}} |
| | [[Image:1kn6.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1kn6| PDB=1kn6 | SCENE= }} | | {{STRUCTURE_1kn6| PDB=1kn6 | SCENE= }} |
|
| |
|
| '''Solution Structure of the Mouse Prohormone Convertase 1 Pro-Domain'''
| | ===Solution Structure of the Mouse Prohormone Convertase 1 Pro-Domain=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| The solution structure of the mouse pro-hormone convertase (PC) 1 pro-domain was determined using heteronuclear NMR spectroscopy and is the first structure to be obtained for any of the domains in the convertase family. The ensemble of NMR-derived structures shows a well-ordered core consisting of a four-stranded antiparallel beta-sheet with two alpha-helices packed against one side of this sheet. Sequence homology suggests that the other eukaryotic PC pro-domains will have the same overall fold and most of the residues forming the hydrophobic core of PC1 are highly conserved within the PC family. However, some of the core residues are predicted by homology to be replaced by polar amino acid residues in other PC pro-domains and this may help to explain their marginal stability. Interestingly, the folding topology observed here is also seen for the pro-domain of bacterial subtilisin despite little or no sequence homology. Both the prokaryotic and eukaryotic structures have hydrophobic residues clustered on the solvent-accessible surface of their beta-sheets although the individual residue types differ. In the bacterial case this region is buried at the binding interface with the catalytic domain and, in the eukaryotic PC family, these surface residues are conserved. We therefore propose that the hydrophobic patch in the PC1 pro-domain is involved in the binding interface with its cognate catalytic domain in a similar manner to that seen for the bacterial system. The PC1 pro-domain structure also reveals potential mechanisms for the acid-induced dissociation of the complex between pro- and catalytic domains.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12095256}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12095256 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_12095256}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| 1KN6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN6 OCA]. | | 1KN6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN6 OCA]. |
|
| |
|
| ==Reference== | | ==Reference== |
| Line 28: |
Line 32: |
| [[Category: Tangrea, M A.]] | | [[Category: Tangrea, M A.]] |
| [[Category: Beta-alpha-beta-beta-alpha-beta]] | | [[Category: Beta-alpha-beta-beta-alpha-beta]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:56:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:35:07 2008'' |