2hqw

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(New page: 200px<br /><applet load="2hqw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hqw, resolution 1.90&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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Calmodulin (CaM) regulates tetrameric N-methyl-D-aspartate receptors, (NMDARs) by binding tightly to the C0 and C1 regions of its NR1 subunit. A, crystal structure (2HQW; 1.96 A) of calcium-saturated CaM bound to NR1C1, (peptide spanning 875-898) showed that NR1 S890, whose phosphorylation, regulates membrane localization, was solvent protected, whereas the, endoplasmic reticulum retention motif was solvent exposed. NR1 F880 filled, the CaM C-domain pocket, whereas T886 was closest to the N-domain pocket., This 1-7 pattern was most similar to that in the CaM-MARCKS complex., Comparison of CaM-ligand wrap-around conformations identified a core, tetrad of CaM C-domain residues (FLMM(C)) that contacted all ligands, consistently. An identical tetrad of N-domain residues (FLMM(N)) made, variable sets of contacts with ligands. This CaM-NR1C1 structure provides, a foundation for designing mutants to test the role of CaM in NR1, trafficking as well as insights into how the homologous CaM domains have, different roles in molecular recognition.
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Calmodulin (CaM) regulates tetrameric N-methyl-D-aspartate receptors (NMDARs) by binding tightly to the C0 and C1 regions of its NR1 subunit. A crystal structure (2HQW; 1.96 A) of calcium-saturated CaM bound to NR1C1 (peptide spanning 875-898) showed that NR1 S890, whose phosphorylation regulates membrane localization, was solvent protected, whereas the endoplasmic reticulum retention motif was solvent exposed. NR1 F880 filled the CaM C-domain pocket, whereas T886 was closest to the N-domain pocket. This 1-7 pattern was most similar to that in the CaM-MARCKS complex. Comparison of CaM-ligand wrap-around conformations identified a core tetrad of CaM C-domain residues (FLMM(C)) that contacted all ligands consistently. An identical tetrad of N-domain residues (FLMM(N)) made variable sets of contacts with ligands. This CaM-NR1C1 structure provides a foundation for designing mutants to test the role of CaM in NR1 trafficking as well as insights into how the homologous CaM domains have different roles in molecular recognition.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences between Homologous Domains., Ataman ZA, Gakhar L, Sorensen BR, Hell JW, Shea MA, Structure. 2007 Dec;15(12):1603-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18073110 18073110]
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The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains., Ataman ZA, Gakhar L, Sorensen BR, Hell JW, Shea MA, Structure. 2007 Dec;15(12):1603-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18073110 18073110]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Akyol, Z.]]
[[Category: Akyol, Z.]]
[[Category: Gakhar, L.]]
[[Category: Gakhar, L.]]
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[[Category: Hell, J.H.]]
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[[Category: Hell, J H.]]
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[[Category: Shea, M.A.]]
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[[Category: Shea, M A.]]
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[[Category: Sorensen, B.R.]]
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[[Category: Sorensen, B R.]]
[[Category: CA]]
[[Category: CA]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
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[[Category: nr1]]
[[Category: nr1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:22:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:54 2008''

Revision as of 15:44, 21 February 2008

Image:2hqw.jpg

2hqw, resolution 1.90Å

Drag the structure with the mouse to rotate

Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide

Overview

Calmodulin (CaM) regulates tetrameric N-methyl-D-aspartate receptors (NMDARs) by binding tightly to the C0 and C1 regions of its NR1 subunit. A crystal structure (2HQW; 1.96 A) of calcium-saturated CaM bound to NR1C1 (peptide spanning 875-898) showed that NR1 S890, whose phosphorylation regulates membrane localization, was solvent protected, whereas the endoplasmic reticulum retention motif was solvent exposed. NR1 F880 filled the CaM C-domain pocket, whereas T886 was closest to the N-domain pocket. This 1-7 pattern was most similar to that in the CaM-MARCKS complex. Comparison of CaM-ligand wrap-around conformations identified a core tetrad of CaM C-domain residues (FLMM(C)) that contacted all ligands consistently. An identical tetrad of N-domain residues (FLMM(N)) made variable sets of contacts with ligands. This CaM-NR1C1 structure provides a foundation for designing mutants to test the role of CaM in NR1 trafficking as well as insights into how the homologous CaM domains have different roles in molecular recognition.

About this Structure

2HQW is a Protein complex structure of sequences from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains., Ataman ZA, Gakhar L, Sorensen BR, Hell JW, Shea MA, Structure. 2007 Dec;15(12):1603-17. PMID:18073110

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