We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2nef

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nef.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2nef.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nef| PDB=2nef | SCENE= }}
{{STRUCTURE_2nef| PDB=2nef | SCENE= }}
-
'''HIV-1 NEF (REGULATORY FACTOR), NMR, 40 STRUCTURES'''
+
===HIV-1 NEF (REGULATORY FACTOR), NMR, 40 STRUCTURES===
-
==Overview==
+
<!--
-
The tendency of HIV-1 Nef to form aggregates in solution, particularly at pH values below 8, together with its large fraction of highly mobile residues seriously complicated determination of its three-dimensional structure, both for heteronuclear solution NMR (Grzesiek et al., 1996a, Nat Struct Biol 3:340-345) and for X-ray crystallography (Lee et al., 1996, Cell 85:931-942). Methods used to determine the Nef structure by NMR at pH 8 and 0.6 mM concentration are presented, together with a detailed description of Nef's secondary and tertiary structure. The described techniques have general applicability for the NMR structure determination of proteins that are aggregating and/or have limited stability at low pH values. Extensive chemical shift assignments are reported for backbone and side chain 1H, 13C, and 15N resonances of the HIV-1 Nef deletion mutants NEF delta 2-39, NEF delta 2-39, delta 159-173, and of NEF delta 2-39, delta 159-173 in complex with the SH3 domain of the Hck tyrosine protein kinase. Besides a type II polyproline helix, Nef's structure consists of three alpha-helices, a 3(10) helix, and a five-stranded anti-parallel beta-sheet. The analysis of 15N relaxation parameters of the backbone amide sites reveals that all the secondary structure elements are non-mobile on the picosecond to nanosecond and on the millisecond time scale. A large number of slowly exchanging amide protons provides evidence for the stability of the Nef core even on the time scale of hours. Significant internal motions on the ps to ns time scale are detected for residues 60 to 71 and for residues 149 to 180, which form solvent-exposed loops. The residues of the HIV-1 protease cleavage site (W57/L58) do not exhibit large amplitude motions on the sub-nanosecond time scale, and their side chains insert themselves into a hydrophobic crevice formed between the C-terminus of helix 1 and the N-terminus of helix 2. A refined structure has been determined based on additional constraints for side-chain and backbone dihedral angles derived from a large number of three-bond J-coupling and ROE data.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9194185}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9194185 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9194185}}
==About this Structure==
==About this Structure==
-
2NEF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_bh10) Human immunodeficiency virus type 1 (isolate bh10)]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nef 1nef]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NEF OCA].
+
2NEF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_bh10) Human immunodeficiency virus type 1 (isolate bh10)]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nef 1nef]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NEF OCA].
==Reference==
==Reference==
Line 35: Line 39:
[[Category: Myristylation]]
[[Category: Myristylation]]
[[Category: Regulatory factor]]
[[Category: Regulatory factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:35:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:03:53 2008''

Revision as of 20:03, 27 July 2008

Image:2nef.png

Template:STRUCTURE 2nef

HIV-1 NEF (REGULATORY FACTOR), NMR, 40 STRUCTURES

Template:ABSTRACT PUBMED 9194185

About this Structure

2NEF is a Single protein structure of sequence from Human immunodeficiency virus type 1 (isolate bh10). This structure supersedes the now removed PDB entry 1nef. Full experimental information is available from OCA.

Reference

Refined solution structure and backbone dynamics of HIV-1 Nef., Grzesiek S, Bax A, Hu JS, Kaufman J, Palmer I, Stahl SJ, Tjandra N, Wingfield PT, Protein Sci. 1997 Jun;6(6):1248-63. PMID:9194185

Page seeded by OCA on Sun Jul 27 23:03:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nef"
Personal tools