1qmu
From Proteopedia
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| - | [[Image:1qmu.jpg|left|200px]]<br /><applet load="1qmu" size=" | + | [[Image:1qmu.jpg|left|200px]]<br /><applet load="1qmu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qmu, resolution 2.70Å" /> | caption="1qmu, resolution 2.70Å" /> | ||
'''DUCK CARBOXYPEPTIDASE D DOMAIN II'''<br /> | '''DUCK CARBOXYPEPTIDASE D DOMAIN II'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_specularioides Anas specularioides] with SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ZN:Zn Binding Site'>ZN</scene>. Full crystallographic information is available from [http:// | + | 1QMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_specularioides Anas specularioides] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ZN:Zn+Binding+Site'>ZN</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-dependent protease]] | [[Category: zinc-dependent protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:01:13 2008'' |
Revision as of 08:01, 3 February 2008
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DUCK CARBOXYPEPTIDASE D DOMAIN II
Overview
The crystal structure of domain II of duck carboxypeptidase D, a, prohormone/propeptide processing enzyme integrated in a three repeat, tandem in the natural system, has been solved, constituting a prototype, for members of the regulatory metallocarboxypeptidase subfamily. It, displays a 300 residue N-terminal alpha/beta-hydrolase subdomain with, overall topological similarity to and general coincidence of the key, catalytic residues with the archetypal pancreatic carboxypeptidase A., However, numerous significant insertions/deletions in segments forming the, funnel-like access to the active site explain differences in specificity, towards larger protein substrates or inhibitors. This alpha/beta-hydrolase, subdomain is followed by a C-terminal 80 residue beta-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to, transthyretin and sugar-binding proteins. The structure described here, establishes the fundamentals for a better understanding of the mechanism, ruling events such as prohormone processing and will enable modelling of, regulatory carboxypeptidases as well as a more rational design of, inhibitors of carboxypeptidase D.
About this Structure
1QMU is a Single protein structure of sequence from Anas specularioides with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily., Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M, EMBO J. 1999 Nov 1;18(21):5817-26. PMID:10545093
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