1niw
From Proteopedia
(New page: 200px<br /> <applet load="1niw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1niw, resolution 2.05Å" /> '''Crystal structure o...) |
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| - | [[Image:1niw. | + | [[Image:1niw.jpg|left|200px]]<br /><applet load="1niw" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1niw, resolution 2.05Å" /> | caption="1niw, resolution 2.05Å" /> | ||
'''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin'''<br /> | '''Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin'''<br /> | ||
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==Disease== | ==Disease== | ||
| - | Known diseases associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Coronary spasms, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Hypertension, pregnancy-induced OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Hypertension, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Placental abruption OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]] | + | Known diseases associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Coronary spasms, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Hypertension, pregnancy-induced OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Hypertension, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Ischemic stroke, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]], Placental abruption OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=163729 163729]] |
==About this Structure== | ==About this Structure== | ||
| - | 1NIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA, SO4 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http:// | + | 1NIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nos]] | [[Category: nos]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:29:10 2008'' |
Revision as of 14:29, 15 February 2008
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Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin
Contents |
Overview
The enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by, the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a, key signaling molecule and cytotoxin. The differential activation of NOS, isozymes by CaM has remained enigmatic, despite extensive research. Here, the crystallographic structure of Ca(2+)-loaded CaM bound to a 20 residue, peptide comprising the endothelial NOS (eNOS) CaM-binding region, establishes their individual conformations and intermolecular, interactions, and suggests the basis for isozyme-specific differences. The, alpha-helical eNOS peptide binds in an antiparallel orientation to CaM, through extensive hydrophobic interactions. Unique NOS interactions occur, with: (i). the CaM flexible central linker, explaining its importance in, NOS activation; and (ii). the CaM C-terminus, explaining the NOS-specific, requirement for a bulky, hydrophobic residue at position 144. This binding, mode expands mechanisms for CaM-mediated activation, explains eNOS, deactivation by Thr495 phosphorylation, and implicates specific, hydrophobic residues in the Ca(2+) independence of inducible NOS.
Disease
Known diseases associated with this structure: Alzheimer disease, late-onset, susceptibility to OMIM:[163729], Coronary spasms, susceptibility to OMIM:[163729], Hypertension, pregnancy-induced OMIM:[163729], Hypertension, susceptibility to OMIM:[163729], Ischemic stroke, susceptibility to OMIM:[163729], Placental abruption OMIM:[163729]
About this Structure
1NIW is a Protein complex structure of sequences from Rattus norvegicus with , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
Reference
Structural basis for endothelial nitric oxide synthase binding to calmodulin., Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, EMBO J. 2003 Feb 17;22(4):766-75. PMID:12574113
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