1ib1

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[[Image:1ib1.gif|left|200px]]
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{{STRUCTURE_1ib1| PDB=1ib1 | SCENE= }}
{{STRUCTURE_1ib1| PDB=1ib1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX'''
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===CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX===
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==Overview==
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Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin synthesis. When isolated from tissue, AANAT copurifies with isoforms epsilon and zeta of 14-3-3. We have determined the structure of AANAT bound to 14-3-3zeta, an association that is phosphorylation dependent. AANAT is bound in the central channel of the 14-3-3zeta dimer, and is held in place by extensive interactions both with the amphipathic phosphopeptide binding groove of 14-3-3zeta and with other parts of the central channel. Thermodynamic and activity measurements, together with crystallographic analysis, indicate that binding of AANAT by 14-3-3zeta modulates AANAT's activity and affinity for its substrates by stabilizing a region of AANAT involved in substrate binding.
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The line below this paragraph, {{ABSTRACT_PUBMED_11336675}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11336675 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11336675}}
==About this Structure==
==About this Structure==
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[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:47:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:41:39 2008''

Revision as of 07:41, 1 July 2008

Template:STRUCTURE 1ib1

CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX

Template:ABSTRACT PUBMED 11336675

About this Structure

1IB1 is a Protein complex structure of sequences from Homo sapiens and Ovis aries. Full crystallographic information is available from OCA.

Reference

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation., Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F, Cell. 2001 Apr 20;105(2):257-67. PMID:11336675

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