NMR paper The serum albumin-binding domain of streptococcal protein G is a three-helical bundle

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[NMR paper] The serum albumin-binding domain of streptococcal protein G is a three-helical bundle

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

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08-22-2010, 02:27 PM

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The serum albumin-binding domain of streptococcal protein G is a three-helical bundle

The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study.

Related Articles The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study.

FEBS Lett. 1996 Jan 8;378(2):190-4

Authors: Kraulis PJ, Jonasson P, Nygren PA, UhlÃ©n M, Jendeberg L, Nilsson B, KÃ¶rdel J

Streptococcal protein G (SPG) is a cell surface receptor protein with a multiple domain structure containing tandem repeats of serum albumin-binding domains (ABD) and immunoglobulin-binding domains (IgBD). In this paper, we have analysed the fold of ABD. Far-UV circular dichroism analysis of ABD indicates high helical content (56%). Based on an analysis of nuclear magnetic resonance 13C secondary chemical shifts, sequential and short-range NOEs, and a few key nuclear Overhauser effects, we conclude that the ABD is a three-helix bundle. The structure of the ABD is, thus, quite different from the IgBD of protein G [Gronenborn, A.M. et al. (1991) Science 253, 657-661]. This strongly suggests that the ABD and the IgBD of SPG have evolved independently from each other. However, the fold of ABD is similar to that of the IgBD of staphylococcal protein A, possibly indicating a common evolutionary ancestor, despite the lack of sequence homology.

PMID: 8549831 [PubMed - indexed for MEDLINE]

Source: PubMed

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