1bdy
From Proteopedia
(New page: 200px<br /><applet load="1bdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bdy, resolution 2.2Å" /> '''C2 DOMAIN FROM PROTEI...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bdy.gif|left|200px]]<br /><applet load="1bdy" size=" | + | [[Image:1bdy.gif|left|200px]]<br /><applet load="1bdy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bdy, resolution 2.2Å" /> | caption="1bdy, resolution 2.2Å" /> | ||
'''C2 DOMAIN FROM PROTEIN KINASE C DELTA'''<br /> | '''C2 DOMAIN FROM PROTEIN KINASE C DELTA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The protein kinase C (PKC) family of lipid-dependent | + | BACKGROUND: The protein kinase C (PKC) family of lipid-dependent serine/theonine kinases plays a central role in many intracellular eukaryotic signalling events. Members of the novel (delta, epsilon, eta, theta) subclass of PKC isotypes lack the Ca2+ dependence of the conventional PKC isotypes and have an N-terminal C2 domain, originally defined as V0 (variable domain zero). Biochemical data suggest that this domain serves to translocate novel PKC family members to the plasma membrane and may influence binding of PKC activators. RESULTS: The crystal structure of PKC-delta C2 domain indicates an unusual variant of the C2 fold. Structural elements unique to this C2 domain include a helix and a protruding beta hairpin which may contribute basic sequences to a membrane-interaction site. The invariant C2 motif, Pro-X-Trp, where X is any amino acid, forms a short crossover loop, departing radically from its conformation in other C2 structures, and contains a tyrosine phosphorylation site unique to PKC-delta. This loop and two others adopt quite different conformations from the equivalent Ca(2+)-binding loops of phospholipase C-delta and synaptotagmin I, and lack sequences necessary for Ca2+ coordination. CONCLUSIONS: The N-terminal sequence of Ca(2+)-independent novel PKCs defines a divergent example of a C2 structure similar to that of phospholipase C-delta. The Ca(2+)-independent regulation of novel PKCs is explained by major structural and sequence differences resulting in three non-functional Ca(2+)-binding loops. The observed structural variation and position of a tyrosine-phosphorylation site suggest the existence of distinct subclasses of C2-like domains which may have evolved distinct functional roles and mechanisms to interact with lipid membranes. |
==About this Structure== | ==About this Structure== | ||
| - | 1BDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http:// | + | 1BDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDY OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dekker, L | + | [[Category: Dekker, L V.]] |
| - | [[Category: Mcdonald, N | + | [[Category: Mcdonald, N Q.]] |
[[Category: Murray-Rust, J.]] | [[Category: Murray-Rust, J.]] | ||
[[Category: Pappa, H.]] | [[Category: Pappa, H.]] | ||
| - | [[Category: Parker, P | + | [[Category: Parker, P J.]] |
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
[[Category: c2 domain]] | [[Category: c2 domain]] | ||
| Line 28: | Line 28: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:19 2008'' |
Revision as of 09:54, 21 February 2008
|
C2 DOMAIN FROM PROTEIN KINASE C DELTA
Overview
BACKGROUND: The protein kinase C (PKC) family of lipid-dependent serine/theonine kinases plays a central role in many intracellular eukaryotic signalling events. Members of the novel (delta, epsilon, eta, theta) subclass of PKC isotypes lack the Ca2+ dependence of the conventional PKC isotypes and have an N-terminal C2 domain, originally defined as V0 (variable domain zero). Biochemical data suggest that this domain serves to translocate novel PKC family members to the plasma membrane and may influence binding of PKC activators. RESULTS: The crystal structure of PKC-delta C2 domain indicates an unusual variant of the C2 fold. Structural elements unique to this C2 domain include a helix and a protruding beta hairpin which may contribute basic sequences to a membrane-interaction site. The invariant C2 motif, Pro-X-Trp, where X is any amino acid, forms a short crossover loop, departing radically from its conformation in other C2 structures, and contains a tyrosine phosphorylation site unique to PKC-delta. This loop and two others adopt quite different conformations from the equivalent Ca(2+)-binding loops of phospholipase C-delta and synaptotagmin I, and lack sequences necessary for Ca2+ coordination. CONCLUSIONS: The N-terminal sequence of Ca(2+)-independent novel PKCs defines a divergent example of a C2 structure similar to that of phospholipase C-delta. The Ca(2+)-independent regulation of novel PKCs is explained by major structural and sequence differences resulting in three non-functional Ca(2+)-binding loops. The observed structural variation and position of a tyrosine-phosphorylation site suggest the existence of distinct subclasses of C2-like domains which may have evolved distinct functional roles and mechanisms to interact with lipid membranes.
About this Structure
1BDY is a Single protein structure of sequence from Rattus norvegicus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the C2 domain from protein kinase C-delta., Pappa H, Murray-Rust J, Dekker LV, Parker PJ, McDonald NQ, Structure. 1998 Jul 15;6(7):885-94. PMID:9687370
Page seeded by OCA on Thu Feb 21 11:54:19 2008
