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


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1knb|  PDB=1knb  |  SCENE=  }}  
{{STRUCTURE_1knb|  PDB=1knb  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF ADENOVIRUS TYPE 5 FIBER PROTEIN AT 1.7 ANGSTROMS RESOLUTION'''
===CRYSTAL STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF ADENOVIRUS TYPE 5 FIBER PROTEIN AT 1.7 ANGSTROMS RESOLUTION===




==Overview==
<!--  
BACKGROUND: Adenoviral infection begins with the binding of virion to the surface of host cells. Specific attachment is achieved through interactions between host-cell receptors and the adenovirus fiber protein and is mediated by the globular carboxy-terminal domain of the adenovirus fiber protein, termed the carboxy-terminal knob domain. RESULTS: The crystal structure of the carboxy-terminal knob domain of the adenovirus type 5 (Ad5) fiber protein has been determined at 1.7 A resolution. Each knob monomer forms an eight-stranded antiparallel beta-sandwich structure. In the crystal lattice, the knob monomers form closely interacting trimers which possess a deep surface depression centered around the three-fold molecular symmetry axis and three symmetry-related valleys. CONCLUSIONS: The amino acid residues lining the wall of the central surface depression and the three symmetry-related floors of the valleys are strictly conserved in the knob domains of Ad5 and adenovirus type 2 (Ad2) fiber proteins, which share the same cellular receptor. The beta-sandwich structure of the knob monomer demonstrates a unique folding topology which is different from that of other known antiparallel beta-sandwich structures. The large buried surface area and numerous polar interactions in the trimer indicate that this form of the knob protein is predominant in solution, suggesting a possible assembly pathway for the native fiber protein.
The line below this paragraph, {{ABSTRACT_PUBMED_7704534}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7704534 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7704534}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Xia, D.]]
[[Category: Xia, D.]]
[[Category: Cell receptor recognition]]
[[Category: Cell receptor recognition]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:56:39 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:35:23 2008''

Revision as of 07:35, 2 July 2008

File:1knb.png

Template:STRUCTURE 1knb

CRYSTAL STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF ADENOVIRUS TYPE 5 FIBER PROTEIN AT 1.7 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 7704534

About this Structure

1KNB is a Single protein structure of sequence from Human adenovirus 5. Full crystallographic information is available from OCA.

Reference

Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution., Xia D, Henry LJ, Gerard RD, Deisenhofer J, Structure. 1994 Dec 15;2(12):1259-70. PMID:7704534

Page seeded by OCA on Wed Jul 2 10:35:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1knb&oldid=621613"