Related ArticlesCharacterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
We have characterized a membrane protein containing residues P688-T762 of the integrin beta3 subunit, encompassing its transmembrane and cytoplasmic domains, by nuclear magnetic resonance spectroscopy. Under conditions in which it is monomeric in dodecylphosphocholine micelles, the protein consists mainly of alpha-helical structures. An amino-terminal helix corresponding to the beta3 transmembrane helix extends into the membrane-proximal region of the cytoplasmic domain. Moreover, following an apparent hinge at residues H722-D723, residues K725-A735 are mostly alpha-helical. In the presence of membrane-mimicking detergents, the cytoplasmic domain connected to the transmembrane helix is substantially ordered at pH 4.8 and 50 degrees C. Its carboxyl-terminal end takes on a turn-helix configuration characteristic of the immunoreceptor tyrosine-based activation motif. These structural features of the beta3 subunit should help to explain its interaction with numerous cytosolic interacting proteins and begin to illuminate the mechanism of integrin activation.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
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[NMR paper] NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabi
NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
Related Articles NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
J Biomol NMR. 2005 Apr;31(4):351-6
Authors: Iwai H, Forrer P, Plückthun A, Güntert P
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11-25-2010 08:21 PM
[NMR paper] NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupl
NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupled CB1 and CB2 receptors in membrane mimetic dodecylphosphocholine micelles.
Related Articles NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupled CB1 and CB2 receptors in membrane mimetic dodecylphosphocholine micelles.
J Biol Chem. 2005 Feb 4;280(5):3605-12
Authors: Xie XQ, Chen JZ
The fourth cytoplasmic domain, the so-called C-terminal juxtamembrane segment or helix VIII, has been identified in numerous G-protein-coupled...
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11-24-2010 10:03 PM
[NMR paper] Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
Related Articles Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
J Biol Chem. 2002 Apr 5;277(14):12375-81
Authors: Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inze D, Scheek R, Lippens G
Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent...
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11-24-2010 08:49 PM
[NMR paper] Investigating the conformational coupling between the transmembrane and cytoplasmic d
Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
Related Articles Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
FEBS Lett. 2001 Sep 21;505(3):431-5
Authors: Mousson F, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM
PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively...
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11-19-2010 08:44 PM
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1008535/aop/images/medium/bi-2010-008535_0002.gif
Biochemistry
DOI: 10.1021/bi1008535
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09-11-2010 01:25 AM
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Related Articles NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Biochemistry. 2010 Aug 27;
Authors: Fatemi N, Korzhnev DM, VÄ?lyvis A, Sarkar B, Forman-Kay JD
The Wilson disease protein (ATP7B) is a copper-transporting member of the P-type ATPase superfamily, which plays a central role in copper homeostasis and interacts with the copper chaperone Atox1. The N-terminus of ATP7B is comprised of six copper-binding domains (WCBDs), each capable of binding one copper atom in the...
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08-31-2010 09:42 PM
NMR characterization of foldedness for the production of E3 RING domains.
NMR characterization of foldedness for the production of E3 RING domains.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR characterization of foldedness for the production of E3 RING domains.
J Struct Biol. 2010 Aug 2;
Authors: Huang A, de Jong RN, Folkers GE, Boelens R
We summarize the use of NMR spectroscopy in the production and the screening of stability and foldedness of protein domains, and apply it to the RING domains of E3 ubiquitin-ligases. RING domains...
Characterization of the monomeric form of the transmembrane and cytoplasmic domains o
Linear Mode
