1mfs
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1mfs.gif|left|200px]]<br /> | + | [[Image:1mfs.gif|left|200px]]<br /><applet load="1mfs" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mfs" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1mfs" /> | caption="1mfs" /> | ||
'''DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES'''<br /> | '''DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1MFS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1MFS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=MNG:These 4 Residues Are The Zn Binding Ligands Of Second Zn ...'>MNG</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MFS OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 27: | ||
[[Category: zinc knuckle]] | [[Category: zinc knuckle]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:45:38 2007'' |
Revision as of 14:35, 18 December 2007
|
DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES
Overview
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.
About this Structure
1MFS is a Single protein structure of sequence from Human immunodeficiency virus with ZN as ligand. Known structural/functional Site: . Full crystallographic 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 Tue Dec 18 16:45:38 2007
