BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 08-21-2010, 11:16 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Secondary structure of a complement control protein module by two-dimensional 1H NMR.

Secondary structure of a complement control protein module by two-dimensional 1H NMR.

Related Articles Secondary structure of a complement control protein module by two-dimensional 1H NMR.

Biochemistry. 1991 Jan 29;30(4):997-1004

Authors: Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID

The complement control protein (CCP) module (also known as the short consensus repeat) is a consensus sequence of about 60 amino acid residues which is thought to fold independently. It occurs over 140 times in more than 20 extracellular mosaic proteins including 12 proteins of the complement cascade. An isolated CCP module, the 16th repeat from human complement factor H, has been expressed in a yeast vector and shown to fold with the same pattern of disulfide bond formation as is seen in the native protein. Two-dimensional 600-MHz 1H NMR spectra of this module have been recorded at pH 3.3 and 6.0 and analyzed to permit determination of secondary structure in solution. The CCP module comprises two predominantly extended segments (Glu1-His13 and Ala17-Glu27), two segments of double-stranded antiparallel beta-sheet (Gly14-Val16 paired with Tyr31-Cys33 and Gly38-Asp40 paired with Ser57-Ile59), and a short piece of triple-stranded beta-sheet (Glu27-Thr30, Ile44-Leu48, and Lys51-Ser53). Turns occur at Asp22, Gly36, and Glu50, while Gly41-Ala43 appear to form a looped-out segment or bulge. This structure is compared with a secondary structure prediction made on the basis of an alignment scheme of 101 sequences for CCP modules [Perkins, S. J., Haris, P. I., Sim, R. B., & Chapman, D. (1988) Biochemistry 27, 4004-4012]--the experimentally determined secondary structure bears an overall resemblance to the predicted one but differs in the number and position of turns. Some of those amino acid residues which are highly conserved throughout the range of CCP modules appear to play a role in stabilizing the global fold.

PMID: 1824927 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] NMR solution structure of complement-like repeat CR3 from the low density lipoprotein
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin. Related Articles NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin. J Biol Chem. 2000 Feb 4;275(5):3264-9 Authors: Dolmer K, Huang W, Gettins PG We have used NMR methods to determine the...
nmrlearner Journal club 0 11-18-2010 09:15 PM
[NMR paper] NMR studies of a viral protein that mimics the regulators of complement activation.
NMR studies of a viral protein that mimics the regulators of complement activation. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of a viral protein that mimics the regulators of complement activation. J Mol Biol. 1997 Sep 19;272(2):253-65 Authors: Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN Vaccinia virus complement control protein (VCP) is a 243-residue protein that is similar in sequence to the regulators of complement activation; its...
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] The secondary structure of phospholamban: a two-dimensional NMR study.
The secondary structure of phospholamban: a two-dimensional NMR study. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The secondary structure of phospholamban: a two-dimensional NMR study. Biochem Biophys Res Commun. 1995 Dec 26;217(3):1200-7 Authors: Maslennikov IV, Sobol AG, Anagli J, James P, Vorherr T, Arseniev AS, Carafoli E Phospholamban (PLN) is an intrinsic membrane protein of 52 amino acids which regulates the Ca2+ pump of the sarcoplasmic reticulum of heart,...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Secondary structure of myristoylated recoverin determined by three-dimensional hetero
Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch. Related Articles Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch. Biochemistry. 1994 Sep 6;33(35):10743-53 Authors: Ames JB, Tanaka T, Stryer L, Ikura M Recoverin, a new member of the EF-hand superfamily, serves as a Ca2+ sensor in vision. A myristoyl or related N-acyl group is covalently attached at its...
nmrlearner Journal club 0 08-22-2010 03:29 AM
[NMR paper] NMR determination of the secondary structure and the three-dimensional polypeptide ba
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2. FEBS Lett. 1993 Nov 29;335(1):18-26 Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K Nuclear magnetic resonance (NMR)...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] 1H NMR assignment and secondary structure of the cell adhesion type III module of fib
1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Related Articles 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry. 1992 Feb 25;31(7):2068-73 Authors: Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID The secondary structure of the tenth type III module from human fibronectin has been determined using NMR. This type of module appears many times in a wide variety of proteins. The type III module described here contains an...
nmrlearner Journal club 0 08-21-2010 11:41 PM
[NMR paper] Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution
Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution. Eur J Biochem. 1990 Nov 13;193(3):789-99 Authors: Yu C, Lee CS, Chuang LC, Shei YR, Wang CY The 1H-NMR spectra of cobrotoxin, a neurotoxic protein isolated from Formosan cobra Naja naja atra, have been studied by...
nmrlearner Journal club 0 08-21-2010 11:04 PM
[NMR paper] NMR solution structure of complement-like repeat CR8 from the low density lipoprotein
NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein. J Biol Chem. 1999 May 14;274(20):14130-6 Authors: Huang W, Dolmer K, Gettins PG The low density lipoprotein receptor-related protein is a member of the low density...
nmrlearner Journal club 0 08-21-2010 04:03 PM



Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 02:07 AM.


Map