1gd3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gd3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1gd3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gd3| PDB=1gd3 | SCENE= }}
{{STRUCTURE_1gd3| PDB=1gd3 | SCENE= }}
-
'''refined solution structure of human cystatin A'''
+
===refined solution structure of human cystatin A===
-
==Overview==
+
<!--
-
The effect of substituting Pro25, located in the alpha-helical region of the cystatin A structure, with Ser has been studied. The structures of wild type and P25S cystatin A were determined by multidimensional NMR spectroscopy under comparable conditions. These two structures were virtually identical, and the alpha-helix between Glu15-Lys30 exists with uninterrupted continuity, with a slight bend at residue 25. In order to characterize the possible substitution effects of Pro25 with Ser on the alpha-helix, the chemical shifts of the amide nitrogens and protons, the generalized order parameters obtained by the analyses of the 15N-1H relaxation data, the amide proton exchange rates, and the NOE networks among the alpha-helical and surrounding residues were carefully compared. None of these parameters indicated any significant static or dynamic structural differences between the alpha-helical regions of the wild-type and P25S cystatin A proteins. We therefore conclude that our previous structure of the wild-type cystatin A, in which the alpha-helix exhibited a sharp kink at Pro25, must be revised. The asymmetric distribution of hydrophobic interactions between the side-chain residues of the alpha-helix and the rolled beta-sheet surface, as revealed by NOEs, may be responsible for the slight bend of the alpha-helix in both variants and for the destabilized hydrogen bonding of the alpha-helical residues that follow Pro25/Ser25, as evidenced by increased amide exchange rates.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12836678}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12836678 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12836678}}
==About this Structure==
==About this Structure==
-
1GD3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD3 OCA].
+
1GD3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD3 OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Cystatin some]]
[[Category: Cystatin some]]
[[Category: Thiol protease inhibitor]]
[[Category: Thiol protease inhibitor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:26:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:07:15 2008''

Revision as of 02:07, 1 July 2008

Template:STRUCTURE 1gd3

refined solution structure of human cystatin A

Template:ABSTRACT PUBMED 12836678

About this Structure

1GD3 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the alpha-helix conformation?, Shimba N, Kariya E, Tate S, Kaji H, Kainosho M, J Struct Funct Genomics. 2000;1(1):26-42. PMID:12836678

Page seeded by OCA on Tue Jul 1 05:07:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools