1mfs: Difference between revisions

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[[Image:1mfs.gif|left|200px]]
{{Seed}}
[[Image:1mfs.png|left|200px]]


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{{STRUCTURE_1mfs|  PDB=1mfs  |  SCENE=  }}  
{{STRUCTURE_1mfs|  PDB=1mfs  |  SCENE=  }}  


'''DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES'''
===DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES===




==Overview==
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The HIV-1 nucleocapsid protein (NC) contains two CCHC-type zinc knuckle domains that are essential for genome recognition, packaging and infectivity. The solution structure of the protein has been determined independently by three groups. Although the structures of the individual zinc knuckle domains are similar, two of the studies indicated that the knuckles behave as independently folded, non-interacting domains connected by a flexible tether, whereas one study revealed the presence of interknuckle NOE cross-peaks, which were interpreted in terms of a more compact structure in which the knuckles are in close proximity. We have collected multidimensional NMR data for the recombinant, isotopically labeled HIV-1 NC protein, and confirmed the presence of weak interknuckle NOEs. However, the NOE data are not consistent with a single protein conformation. 15N NMR relaxation studies reveal that the two zinc knuckle domains possess different effective rotational correlation times, indicating that the knuckles are not tumbling as a single globular domain. In addition, the 1H NMR chemical shifts of isolated zinc knuckle peptides are very similar to those of the intact protein. The combined results indicate that the interknuckle interactions, which involve the close approach of the side-chains of Phe16 and Trp37, are transitory. The solution behavior of NC may be best considered as a rapid equilibrium between conformations with weakly interacting and non-interacting knuckle domains. This inherent conformational flexibility may be functionally important, enabling adaptive binding of NC to different recognition elements within the HIV-1 psi-RNA packaging signal.
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{{ABSTRACT_PUBMED_9641983}}


==About this Structure==
==About this Structure==
1MFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFS OCA].  
1MFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFS OCA].  


==Reference==
==Reference==
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[[Category: Zinc binding]]
[[Category: Zinc binding]]
[[Category: Zinc knuckle]]
[[Category: Zinc knuckle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:52:44 2008''

Revision as of 20:52, 2 July 2008

File:1mfs.png

Template:STRUCTURE 1mfs

DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES

Template:ABSTRACT PUBMED 9641983

About this Structure

1MFS is a Single protein structure of sequence from Human immunodeficiency virus. Full experimental information is available from OCA.

Reference

Dynamical behavior of the HIV-1 nucleocapsid protein., Lee BM, De Guzman RN, Turner BG, Tjandra N, Summers MF, J Mol Biol. 1998 Jun 12;279(3):633-49. PMID:9641983

Page seeded by OCA on Wed Jul 2 23:52:44 2008

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