1pk8

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{{STRUCTURE_1pk8| PDB=1pk8 | SCENE= }}
{{STRUCTURE_1pk8| PDB=1pk8 | SCENE= }}
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'''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP'''
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===Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP===
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==Overview==
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Synapsins are multidomain proteins that are critical for regulating neurotransmitter release in vertebrates. In the present study, two crystal structures of the C domain of rat synapsin I (rSynI-C) in complex with Ca(2+) and ATP reveal that this protein can form a tetramer and that a flexible loop (the "multifunctional loop") contacts bound ATP. Further experiments were carried out on a protein comprising the A, B, and C domains of rat synapsin I (rSynI-ABC). An ATP-stabilized tetramer of rSynI-ABC is observed during velocity sedimentation and size-exclusion chromatographic experiments. These hydrodynamic results also indicate that the A and B domains exist in an extended conformation. Calorimetric measurements of ATP binding to wild-type and mutant rSynI-ABC demonstrate that the multifunctional loop and a cross-tetramer contact are important for ATP binding. The evidence supports a view of synapsin I as an ATP-utilizing, tetrameric protein made up of monomers that have a flexible, extended N terminus.
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(as it appears on PubMed at http://www.pubmed.gov), where 14688264 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14688264}}
==About this Structure==
==About this Structure==
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[[Category: Atp binding]]
[[Category: Atp binding]]
[[Category: Atp grasp]]
[[Category: Atp grasp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:10:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:57:25 2008''

Revision as of 02:57, 29 July 2008

Template:STRUCTURE 1pk8

Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP

Template:ABSTRACT PUBMED 14688264

About this Structure

1PK8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I., Brautigam CA, Chelliah Y, Deisenhofer J, J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264

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