1rwe: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1rwe.gif|left|200px]]
{{Seed}}
[[Image:1rwe.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rwe|  PDB=1rwe  |  SCENE=  }}  
{{STRUCTURE_1rwe|  PDB=1rwe  |  SCENE=  }}  


'''Enhancing the activity of insulin at receptor edge: crystal structure and photo-cross-linking of A8 analogues'''
===Enhancing the activity of insulin at receptor edge: crystal structure and photo-cross-linking of A8 analogues===




==Overview==
<!--
The receptor-binding surface of insulin is broadly conserved, reflecting its evolutionary optimization. Neighboring positions nevertheless offer an opportunity to enhance activity, through either transmitted structural changes or introduction of novel contacts. Nonconserved residue A8 is of particular interest as Thr(A8) --&gt; His substitution (a species variant in birds and fish) augments the potency of human insulin. Diverse A8 substitutions are well tolerated, suggesting that the hormone-receptor interface is not tightly packed at this site. To resolve whether enhanced activity is directly or indirectly mediated by the variant A8 side chain, we have determined the crystal structure of His(A8)-insulin and investigated the photo-cross-linking properties of an A8 analogue containing p-azidophenylalanine. The structure, characterized as a T(3)R(3)(f) zinc hexamer at 1.8 A resolution, is essentially identical to that of native insulin. The photoactivatable analogue exhibits efficient cross-linking to the insulin receptor. The site of cross-linking lies within a 14 kDa C-terminal domain of the alpha-subunit. This contact, to our knowledge the first to be demonstrated from the A chain, is inconsistent with a recent model of the hormone-receptor complex derived from electron microscopy. Optimizing the binding interaction of a nonconserved side chain on the surface of insulin may thus enhance its activity.
The line below this paragraph, {{ABSTRACT_PUBMED_15610006}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15610006 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15610006}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: A8-histidine human insulin]]
[[Category: A8-histidine human insulin]]
[[Category: Insulin receptor]]
[[Category: Insulin receptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:59:06 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:01:40 2008''

Revision as of 11:01, 29 July 2008

File:1rwe.png

Template:STRUCTURE 1rwe

Enhancing the activity of insulin at receptor edge: crystal structure and photo-cross-linking of A8 analogues

Template:ABSTRACT PUBMED 15610006

About this Structure

1RWE is a Protein complex structure. Full crystallographic information is available from OCA.

Reference

Enhancing the activity of insulin at the receptor interface: crystal structure and photo-cross-linking of A8 analogues., Wan Z, Xu B, Huang K, Chu YC, Li B, Nakagawa SH, Qu Y, Hu SQ, Katsoyannis PG, Weiss MA, Biochemistry. 2004 Dec 28;43(51):16119-33. PMID:15610006

Page seeded by OCA on Tue Jul 29 14:01:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1rwe&oldid=744279"